1qol - Revision history

OCA at 06:05, 17 April 2024

OCA — Wed, 17 Apr 2024 06:05:56 GMT

←Older revision		Revision as of 06:05, 17 April 2024
Line 3:		Line 3:
	<StructureSection load='1qol' size='340' side='right'caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1qol' size='340' side='right'caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Fmdv Fmdv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_(strain_O1) Foot-and-mouth disease virus (strain O1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~, ~~<scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1qmy\|1qmy]]~~, ~~[[1qqp\|1qqp]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [https://pdbe.org/1qol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [https://www.ebi.ac.uk/pdbsum/1qol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qol ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [https://pdbe.org/1qol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [https://www.ebi.ac.uk/pdbsum/1qol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POLG_FMDVO POLG_FMDVO]] The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref>	+	[https://www.uniprot.org/uniprot/POLG_FMDVO POLG_FMDVO] The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qol ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qol ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The leader protease of foot-and-mouth disease virus, as well as cleaving itself from the nascent viral polyprotein, disables host cell protein synthesis by specific proteolysis of a cellular protein: the eukaryotic initiation factor 4G (eIF4G). The crystal structure of the leader protease presented here comprises a globular catalytic domain reminiscent of that of cysteine proteases of the papain superfamily, and a flexible C-terminal extension found intruding into the substrate-binding site of an adjacent molecule. Nevertheless, the relative disposition of this extension and the globular domain to each other supports intramolecular self-processing. The different sequences of the two substrates cleaved during viral replication, the viral polyprotein (at LysLeuLys/GlyAlaGly) and eIF4G (at AsnLeuGly/ArgThrThr), appear to be recognized by distinct features in a narrow, negatively charged groove traversing the active centre. The structure illustrates how the prototype papain fold has been adapted to the requirements of an RNA virus. Thus, the protein scaffold has been reduced to a minimum core domain, with the active site being modified to increase specificity. Furthermore, surface features have been developed which enable C-terminal self-processing from the viral polyprotein.
-
-	Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.,Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T EMBO J. 1998 Dec 15;17(24):7469-79. PMID:9857201<ref>PMID:9857201</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Fmdv]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fita, I]]	+	[[Category: Fita I]]
-	[[Category: Guarne, A]]	+	[[Category: Guarne A]]
-	[[Category: Kirchweger, R]]	+	[[Category: Kirchweger R]]
-	[[Category: Pfistermueller, D]]	+	[[Category: Pfistermueller D]]
-	[[Category: Skern, T]]	+	[[Category: Skern T]]
-	[[Category: Tormo, J]]	+	[[Category: Tormo J]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Picornaviral proteinase]]~~	+
-	~~[[Category: Sulfhydryl proteinase~~]]	+

OCA at 06:03, 28 April 2021

OCA — Wed, 28 Apr 2021 06:03:21 GMT

←Older revision		Revision as of 06:03, 28 April 2021
Line 3:		Line 3:
	<StructureSection load='1qol' size='340' side='right'caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1qol' size='340' side='right'caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1QOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qmy\|1qmy]], [[1qqp\|1qqp]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [~~http~~://pdbe.org/1qol PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1qol PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1qol ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [https://pdbe.org/1qol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [https://www.ebi.ac.uk/pdbsum/1qol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POLG_FMDVO POLG_FMDVO]] The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref>	+	[[https://www.uniprot.org/uniprot/POLG_FMDVO POLG_FMDVO]] The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Nonstructural protein\|Nonstructural protein]]	+	*[[Nonstructural protein 3D structures\|Nonstructural protein 3D structures]]
		+	*[[Virus protease 3D structures\|Virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:00, 24 July 2019

OCA — Wed, 24 Jul 2019 07:00:08 GMT

←Older revision		Revision as of 07:00, 24 July 2019
Line 1:		Line 1:

	==STRUCTURE OF THE FMDV LEADER PROTEASE==		==STRUCTURE OF THE FMDV LEADER PROTEASE==
-	<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='1qol' size='340' side='right'caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Nonstructural protein\|Nonstructural protein]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Fmdv]]		[[Category: Fmdv]]
		+	[[Category: Large Structures]]
	[[Category: Fita, I]]		[[Category: Fita, I]]
	[[Category: Guarne, A]]		[[Category: Guarne, A]]

OCA at 07:46, 28 February 2018

OCA — Wed, 28 Feb 2018 07:46:06 GMT

←Older revision		Revision as of 07:46, 28 February 2018
Line 1:		Line 1:
		+
	==STRUCTURE OF THE FMDV LEADER PROTEASE==		==STRUCTURE OF THE FMDV LEADER PROTEASE==
	<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://pdbe.org/1qol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://pdbe.org/1qol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/1qol_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/1qol_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Nonstructural protein\|Nonstructural protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:38, 8 February 2016

OCA — Mon, 08 Feb 2016 14:38:21 GMT

←Older revision		Revision as of 14:38, 8 February 2016
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qol ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 12:34, 10 September 2015

OCA — Thu, 10 Sep 2015 12:34:10 GMT

←Older revision		Revision as of 12:34, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://pdbe.org/1qol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1qol" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Fmdv]]
	[[Category: Fita, I]]		[[Category: Fita, I]]
	[[Category: Guarne, A]]		[[Category: Guarne, A]]

OCA at 00:04, 25 December 2014

OCA — Thu, 25 Dec 2014 00:04:24 GMT

←Older revision		Revision as of 00:04, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_FMDVO POLG_FMDVO]] The leader protease autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. It also cleaves the host translation initiation factor EIF4G1 and EIF4G3, in order to shut down the capped cellular mRNA transcription.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The capsid interacts with host heparan sulfate and various integrins (alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8) to provide virion attachment to target Attachment via host integrins induces virion internalization predominantly through clathrin-mediated endocytosis. In strains adapted to cell culture, attachment to heparan sulfate can also be used and induces virion internalization through clathrin- and caveolin-independent endocytosis.<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein VP0: VP0 precursor is a component of immature procapsids (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2B: Affects membrane integrity and cause an increase in membrane permeability (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3A, via its hydrophobic domain, serves as membrane anchor (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. They acts as a genome-linked replication primer (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref> RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).<ref>PMID:8386879</ref> <ref>PMID:11034318</ref> <ref>PMID:15016848</ref> <ref>PMID:18614639</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Fita, I.]]	+	[[Category: Fita, I]]
-	[[Category: Guarne, A.]]	+	[[Category: Guarne, A]]
-	[[Category: Kirchweger, R.]]	+	[[Category: Kirchweger, R]]
-	[[Category: Pfistermueller, D.]]	+	[[Category: Pfistermueller, D]]
-	[[Category: Skern, T.]]	+	[[Category: Skern, T]]
-	[[Category: Tormo, J.]]	+	[[Category: Tormo, J]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Picornaviral proteinase]]		[[Category: Picornaviral proteinase]]
	[[Category: Sulfhydryl proteinase]]		[[Category: Sulfhydryl proteinase]]

OCA at 21:41, 28 September 2014

OCA — Sun, 28 Sep 2014 21:41:14 GMT

←Older revision		Revision as of 21:41, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1qol.~~png~~\|~~left~~\|200px]]	+	==STRUCTURE OF THE FMDV LEADER PROTEASE==
		+	<StructureSection load='1qol' size='340' side='right' caption='[[1qol]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QOL FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qmy\|1qmy]], [[1qqp\|1qqp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qol RCSB], [http://www.ebi.ac.uk/pdbsum/1qol PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qo/1qol_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The leader protease of foot-and-mouth disease virus, as well as cleaving itself from the nascent viral polyprotein, disables host cell protein synthesis by specific proteolysis of a cellular protein: the eukaryotic initiation factor 4G (eIF4G). The crystal structure of the leader protease presented here comprises a globular catalytic domain reminiscent of that of cysteine proteases of the papain superfamily, and a flexible C-terminal extension found intruding into the substrate-binding site of an adjacent molecule. Nevertheless, the relative disposition of this extension and the globular domain to each other supports intramolecular self-processing. The different sequences of the two substrates cleaved during viral replication, the viral polyprotein (at LysLeuLys/GlyAlaGly) and eIF4G (at AsnLeuGly/ArgThrThr), appear to be recognized by distinct features in a narrow, negatively charged groove traversing the active centre. The structure illustrates how the prototype papain fold has been adapted to the requirements of an RNA virus. Thus, the protein scaffold has been reduced to a minimum core domain, with the active site being modified to increase specificity. Furthermore, surface features have been developed which enable C-terminal self-processing from the viral polyprotein.

-	~~{{STRUCTURE_1qol\| PDB=1qol \| SCENE= }}~~	+	Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition.,Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T EMBO J. 1998 Dec 15;17(24):7469-79. PMID:9857201<ref>PMID:9857201</ref>

-	~~===STRUCTURE OF THE FMDV LEADER PROTEASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9857201}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1qol]] is~~ a ~~8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA].~~	+

	==See Also==		==See Also==
	*[[Nonstructural protein\|Nonstructural protein]]		*[[Nonstructural protein\|Nonstructural protein]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:009857201<~~/~~ref~~><~~ref group="xtra">PMID:009472614</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Fita, I.]]		[[Category: Fita, I.]]
	[[Category: Guarne, A.]]		[[Category: Guarne, A.]]

OCA at 10:29, 20 October 2012

OCA — Sat, 20 Oct 2012 10:29:03 GMT

←Older revision		Revision as of 10:29, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1qol]] is a 8 chain structure ~~of [[Nonstructural protein]]~~ with sequence from [http://en.wikipedia.org/wiki/Foot-and-~~mouth_disease_virus~~ Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA].	+	[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_(strain_o1) Foot-and-mouth disease virus (strain o1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA].

	==See Also==		==See Also==
Line 15:		Line 15:
	==Reference==		==Reference==
	<ref group="xtra">PMID:009857201</ref><ref group="xtra">PMID:009472614</ref><references group="xtra"/>		<ref group="xtra">PMID:009857201</ref><ref group="xtra">PMID:009472614</ref><references group="xtra"/>
-	[[Category: Foot-and-mouth disease virus]]
	[[Category: Fita, I.]]		[[Category: Fita, I.]]
	[[Category: Guarne, A.]]		[[Category: Guarne, A.]]

OCA at 02:16, 26 July 2012

OCA — Thu, 26 Jul 2012 02:16:20 GMT

←Older revision		Revision as of 02:16, 26 July 2012
Line 1:		Line 1:
	[[Image:1qol.png\|left\|200px]]		[[Image:1qol.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1qol", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1qol\| PDB=1qol \| SCENE= }}		{{STRUCTURE_1qol\| PDB=1qol \| SCENE= }}

	===STRUCTURE OF THE FMDV LEADER PROTEASE===		===STRUCTURE OF THE FMDV LEADER PROTEASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9857201}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9857201 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_9857201}}		{{ABSTRACT_PUBMED_9857201}}

	==About this Structure==		==About this Structure==
-	[[1qol]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA].	+	[[1qol]] is a 8 chain structure of [[Nonstructural protein]] with sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA].
		+
		+	==See Also==
		+	*[[Nonstructural protein\|Nonstructural protein]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9857201~~</ref><ref group="xtra">PMID:~~9472614~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009857201</ref><ref group="xtra">PMID:009472614</ref><references group="xtra"/>
	[[Category: Foot-and-mouth disease virus]]		[[Category: Foot-and-mouth disease virus]]
	[[Category: Fita, I.]]		[[Category: Fita, I.]]