4q4g - Revision history

OCA at 12:44, 1 March 2024

2024-03-01T12:44:01Z

←Older revision		Revision as of 12:44, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
-	</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [https://pdbe.org/4q4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [https://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></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]] 0.97Å</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [https://pdbe.org/4q4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [https://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref>		[https://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	RipA is a key cysteine protease of Mycobacterium tuberculosis as it is responsible for bacterial daughter-cell separation. Although it is an important target for antimicrobial development, its mechanism of action and its interaction pattern with its substrate are hitherto unknown. By combining crystallographic and mutational studies with functional assays and molecular modelling, it is shown that the catalytic activity of the enzyme relies on a Cys-His-Glu triad and the impact of the mutation of each residue of the triad on the structure and function of RipA is analysed. Unexpectedly, the crystallographic analyses reveal that mutation of the glutamic acid to alanine results in inversion of the configuration of the catalytic cysteine. The consequent burial of the catalytic cysteine side chain explains the enzyme inactivation upon mutation. These data point to a novel role of the acidic residue often present in the triad of cysteine proteases as a supervisor of cysteine configuration through preservation of the local structural integrity.
-
-	Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine.,Squeglia F, Ruggiero A, Romano M, Vitagliano L, Berisio R Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2295-300. doi:, 10.1107/S1399004714013674. Epub 2014 Aug 29. PMID:25195744<ref>PMID:25195744</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4q4g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:43, 8 February 2023

2023-02-08T07:43:22Z

←Older revision		Revision as of 07:43, 8 February 2023
Line 3:		Line 3:
	<StructureSection load='4q4g' size='340' side='right'caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>		<StructureSection load='4q4g' size='340' side='right'caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus~~ tuberculosis~~" (zopf 1883) klein 1884~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</td></tr>~~	+	</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [https://pdbe.org/4q4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [https://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ripA, Rv1477 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [~~http~~://pdbe.org/4q4g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU]] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref>	+	[https://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Berisio, R~~]]	+	[[Category: Mycobacterium tuberculosis]]
-	[[Category: ~~Alpha-beta]]~~	+	[[Category: Berisio R]]
-	~~[[Category: Cell wall hydrolase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 08:46, 24 April 2019

2019-04-24T08:46:10Z

←Older revision		Revision as of 08:46, 24 April 2019
Line 1:		Line 1:

	==Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383==		==Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383==
-	<StructureSection load='4q4g' size='340' side='right' caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>	+	<StructureSection load='4q4g' size='340' side='right'caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ripA, Rv1477 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://pdbe.org/4q4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://pdbe.org/4q4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></td></tr>
	</table>		</table>
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Berisio, R]]		[[Category: Berisio, R]]
	[[Category: Alpha-beta]]		[[Category: Alpha-beta]]
	[[Category: Cell wall hydrolase]]		[[Category: Cell wall hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 20:13, 4 August 2016

2016-08-04T20:13:52Z

←Older revision		Revision as of 20:13, 4 August 2016
Line 1:		Line 1:
		+
	==Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383==		==Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383==
	<StructureSection load='4q4g' size='340' side='right' caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>		<StructureSection load='4q4g' size='340' side='right' caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g 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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://pdbe.org/4q4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q4g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4q4g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:45, 25 December 2014

2014-12-25T12:45:00Z

←Older revision		Revision as of 12:45, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>		<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g 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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RIPA_MYCTU RIPA_MYCTU]] Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds and degrades high-molecular weight peptidoglycan from a number of Actinobacteria; activity is increased in the presence of RpfB and inhibited by PBP1A (ponA1). Required for normal separation of daughter cells after cell division and for cell wall integrity. Required for host cell invasion and intracellular survival in host macrophages.<ref>PMID:16495549</ref> <ref>PMID:17919286</ref> <ref>PMID:18463693</ref> <ref>PMID:20826344</ref> <ref>PMID:21864539</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Berisio, R.]]	+	[[Category: Berisio, R]]
	[[Category: Alpha-beta]]		[[Category: Alpha-beta]]
	[[Category: Cell wall hydrolase]]		[[Category: Cell wall hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 05:43, 24 September 2014

2014-09-24T05:43:59Z

←Older revision		Revision as of 05:43, 24 September 2014
Line 6:		Line 6:
	<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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum]</span></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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	RipA is a key cysteine protease of Mycobacterium tuberculosis as it is responsible for bacterial daughter-cell separation. Although it is an important target for antimicrobial development, its mechanism of action and its interaction pattern with its substrate are hitherto unknown. By combining crystallographic and mutational studies with functional assays and molecular modelling, it is shown that the catalytic activity of the enzyme relies on a Cys-His-Glu triad and the impact of the mutation of each residue of the triad on the structure and function of RipA is analysed. Unexpectedly, the crystallographic analyses reveal that mutation of the glutamic acid to alanine results in inversion of the configuration of the catalytic cysteine. The consequent burial of the catalytic cysteine side chain explains the enzyme inactivation upon mutation. These data point to a novel role of the acidic residue often present in the triad of cysteine proteases as a supervisor of cysteine configuration through preservation of the local structural integrity.
		+
		+	Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine.,Squeglia F, Ruggiero A, Romano M, Vitagliano L, Berisio R Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2295-300. doi:, 10.1107/S1399004714013674. Epub 2014 Aug 29. PMID:25195744<ref>PMID:25195744</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:13, 10 September 2014

2014-09-10T10:13:44Z

←Older revision		Revision as of 10:13, 10 September 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383==
-		+	<StructureSection load='4q4g' size='340' side='right' caption='[[4q4g]], [[Resolution\|resolution]] 0.97Å' scene=''>
-	~~The entry~~ 4q4g is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4q4g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q4G FirstGlance]. <br>
-	~~Authors~~: Berisio, R.	+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4q4n\|4q4n]], [[4q4t\|4q4t]]</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=4q4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q4g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q4g RCSB], [http://www.ebi.ac.uk/pdbsum/4q4g PDBsum]</span></td></tr>
-	~~Description~~: ~~Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383~~	+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Berisio, R.]]
		+	[[Category: Alpha-beta]]
		+	[[Category: Cell wall hydrolase]]
		+	[[Category: Hydrolase]]

OCA: Protected "4q4g" [edit=sysop:move=sysop]

2014-04-23T07:29:38Z

Protected "4q4g" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:29, 23 April 2014

OCA: New page: '''Unreleased structure''' The entry 4q4g is ON HOLD Authors: Berisio, R. Description: Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383

2014-04-23T07:29:37Z

New page: '''Unreleased structure''' The entry 4q4g is ON HOLD Authors: Berisio, R. Description: Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383

New page

'''Unreleased structure'''

The entry 4q4g is ON HOLD

Authors: Berisio, R.

Description: Structure of the Resuscitation Promoting Factor Interacting protein RipA mutated at C383