2jqg
From Proteopedia
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==Leader Protease== | ==Leader Protease== | ||
| - | <StructureSection load='2jqg' size='340' side='right' caption='[[2jqg | + | <StructureSection load='2jqg' size='340' side='right'caption='[[2jqg]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2jqg]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2jqg]] is a 1 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 experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqg OCA], [https://pdbe.org/2jqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqg RCSB], [https://www.ebi.ac.uk/pdbsum/2jqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqg 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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/2jqg_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/2jqg_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> | ||
</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/ | + | </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=2jqg ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 2jqg" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Cencic | + | [[Category: Cencic R]] |
| - | [[Category: Juliano | + | [[Category: Juliano L]] |
| - | [[Category: Juliano | + | [[Category: Juliano MA]] |
| - | [[Category: Konrat | + | [[Category: Konrat R]] |
| - | [[Category: Kontaxis | + | [[Category: Kontaxis G]] |
| - | [[Category: Mayer | + | [[Category: Mayer C]] |
| - | [[Category: Skern | + | [[Category: Skern T]] |
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Current revision
Leader Protease
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Categories: Large Structures | Cencic R | Juliano L | Juliano MA | Konrat R | Kontaxis G | Mayer C | Skern T
