4g4e - Revision history

OCA at 13:56, 8 November 2023

2023-11-08T13:56:24Z

← Older revision		Revision as of 13:56, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G4E 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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [https://pdbe.org/4g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [https://www.ebi.ac.uk/pdbsum/4g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4e 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]] 2.888Å</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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [https://pdbe.org/4g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [https://www.ebi.ac.uk/pdbsum/4g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 20:24, 19 October 2022

2022-10-19T20:24:00Z

← Older revision		Revision as of 20:24, 19 October 2022
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	==Crystal structure of the L88A mutant of HslV from Escherichia coli==		==Crystal structure of the L88A mutant of HslV from Escherichia coli==
	<StructureSection load='4g4e' size='340' side='right' caption='[[4g4e]], [[Resolution\|resolution]] 2.89Å' scene=''>		<StructureSection load='4g4e' size='340' side='right'caption='[[4g4e]], [[Resolution\|resolution]] 2.89Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G4E FirstGlance]. <br>
	</td></tr>~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hslV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [https://pdbe.org/4g4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [https://www.ebi.ac.uk/pdbsum/4g4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4e ProSAT]</span></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HslU--HslV_peptidase HslU--HslV peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.2 3.4.25.2] </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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [~~http~~://pdbe.org/4g4e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g4e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref>		[https://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4g4e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4g4e" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Ecoli~~]]		[[Category: Escherichia coli K-12]]
	[[Category: ~~HslU--HslV peptidase~~]]		[[Category: Large Structures]]
	[[Category: An~~, J Y~~]]		[[Category: An JY]]
	[[Category: Chung~~, C H~~]]		[[Category: Chung CH]]
	[[Category: Eom~~, S H~~]]		[[Category: Eom SH]]
	[[Category: Ha~~, B H~~]]		[[Category: Ha BH]]
	[[Category: Jeon~~, Y J~~]]		[[Category: Jeon YJ]]
	[[Category: Lee~~, J W~~]]		[[Category: Lee JW]]
	[[Category: Park, E]]		[[Category: Park E]]
	[[Category: Seol~~, J H~~]]		[[Category: Seol JH]]
	[[Category: Yoo~~, H M]]~~		[[Category: Yoo HM]]
	~~[[Category: Atp-dependent protease]]~~
	~~[[Category: Hslu atpase]]~~
	~~[[Category: Hslv protease]]~~
	~~[[Category: Hslvu]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Pore motif~~]]

OCA at 13:40, 5 August 2016

2016-08-05T13:40:20Z

← Older revision		Revision as of 13:40, 5 August 2016
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	==Crystal structure of the L88A mutant of HslV from Escherichia coli==		==Crystal structure of the L88A mutant of HslV from Escherichia coli==
	<StructureSection load='4g4e' size='340' side='right' caption='[[4g4e]], [[Resolution\|resolution]] 2.89Å' scene=''>		<StructureSection load='4g4e' size='340' side='right' caption='[[4g4e]], [[Resolution\|resolution]] 2.89Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G4E FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hslV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hslV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HslU--HslV_peptidase HslU--HslV peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.2 3.4.25.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HslU--HslV_peptidase HslU--HslV peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.2 3.4.25.2] </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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [http://www.ebi.ac.uk/pdbsum/4g4e 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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [http://pdbe.org/4g4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [http://www.ebi.ac.uk/pdbsum/4g4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4g4e" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Escherichia coli k-12~~]]		[[Category: Ecoli]]
	[[Category: HslU--HslV peptidase]]		[[Category: HslU--HslV peptidase]]
	[[Category: An, J Y]]		[[Category: An, J Y]]

OCA at 19:16, 25 December 2014

2014-12-25T19:16:18Z

← Older revision		Revision as of 19:16, 25 December 2014
Line 7:		Line 7:
	<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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [http://www.ebi.ac.uk/pdbsum/4g4e 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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [http://www.ebi.ac.uk/pdbsum/4g4e PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:22, 21 December 2014

2014-12-21T11:22:14Z

← Older revision		Revision as of 11:22, 21 December 2014
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	~~{{STRUCTURE_4g4e\| PDB=4g4e \| SCENE= }}~~		==Crystal structure of the L88A mutant of HslV from Escherichia coli==
	===Crystal structure of the L88A mutant of HslV from Escherichia coli===		<StructureSection load='4g4e' size='340' side='right' caption='[[4g4e]], [[Resolution\|resolution]] 2.89Å' scene=''>
	~~{{ABSTRACT_PUBMED_23707406}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4g4e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G4E FirstGlance]. <br>
			</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hslV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/HslU--HslV_peptidase HslU--HslV peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.2 3.4.25.2] </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=4g4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g4e RCSB], [http://www.ebi.ac.uk/pdbsum/4g4e PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In all cells, ATP-dependent proteases play central roles in the controlled degradation of short-lived regulatory or misfolded proteins. A hallmark of these enzymes is that proteolytic active sites are sequestered within a compartmentalized space, which is accessible to substrates only when they are fed into the cavity by protein-unfolding ATPases. HslVU is a prototype of such enzymes, consisting of the hexameric HslU ATPase and the dodecameric HslV protease. HslV forms a barrel-shaped proteolytic chamber with two constricted axial pores. Here, we report that structural alterations of HslV's pore motif dramatically affect the proteolytic activities of both HslV and HslVU complexes. Mutations of a conserved pore residue in HslV (Leu88 to Ala, Gly, or Ser) led to a tighter binding between HslV and HslU and a dramatic stimulation of both the proteolytic and ATPase activities. Furthermore, the HslV mutants alone showed a marked increase of basal hydrolytic activities toward small peptides and unstructured proteins. A synthetic peptide of the HslU C-terminal tail further stimulated the proteolytic activities of these mutants, even allowing degradation of certain folded proteins in the absence of HslU. Moreover, expression of the L88A mutant in Escherichia coli inhibited cell growth, suggesting that HslV pore mutations dysregulate the protease through relaxing the pore constriction, which normally prevents essential cellular proteins from random degradation. Consistent with these observations, an X-ray crystal structure shows that the pore loop of L88A-HslV is largely disordered. Collectively, these results suggest that substrate degradation by HslV is controlled by gating of its pores.

	~~==Function==~~		Structural Alteration in the Pore Motif of the Bacterial 20S Proteasome Homolog HslV Leads to Uncontrolled Protein Degradation.,Park E, Lee JW, Yoo HM, Ha BH, An JY, Jeon YJ, Seol JH, Eom SH, Chung CH J Mol Biol. 2013 May 21. pii: S0022-2836(13)00310-0. doi:, 10.1016/j.jmb.2013.05.011. PMID:23707406<ref>PMID:23707406</ref>
	[[http://www.uniprot.org/uniprot/HSLV_ECOLI HSLV_ECOLI]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the ~~specific degradation~~ of ~~heat shock induced transcription factors such as RpoH and SulA~~. ~~In addition~~, ~~small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU~~, ~~but this activity is induced more than 100-fold in the presence of HslU~~. ~~HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis~~. ~~HslV is not believed to degrade folded proteins~~.~~<ref>PMID~~:~~8662828<~~/~~ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>~~PMID:~~10419524</ref>~~ <ref>PMID:~~15696175~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4g4e]] is~~ a ~~12 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4G4E OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:023707406</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: HslU--HslV peptidase]]		[[Category: HslU--HslV peptidase]]
	[[Category: An, J Y.]]		[[Category: An, J Y]]
	[[Category: Chung, C H.]]		[[Category: Chung, C H]]
	[[Category: Eom, S H.]]		[[Category: Eom, S H]]
	[[Category: Ha, B H.]]		[[Category: Ha, B H]]
	[[Category: Jeon, Y J.]]		[[Category: Jeon, Y J]]
	[[Category: Lee, J W.]]		[[Category: Lee, J W]]
	[[Category: Park, E.]]		[[Category: Park, E]]
	[[Category: Seol, J H.]]		[[Category: Seol, J H]]
	[[Category: Yoo, H M.]]		[[Category: Yoo, H M]]
	[[Category: Atp-dependent protease]]		[[Category: Atp-dependent protease]]
	[[Category: Hslu atpase]]		[[Category: Hslu atpase]]

OCA at 06:27, 14 August 2013

2013-08-14T06:27:30Z

← Older revision		Revision as of 06:27, 14 August 2013
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	[[Category: Jeon, Y J.]]		[[Category: Jeon, Y J.]]
	[[Category: Lee, J W.]]		[[Category: Lee, J W.]]
	[[Category: Park, E]]		[[Category: Park, E.]]
	[[Category: Seol, J H.]]		[[Category: Seol, J H.]]
	[[Category: Yoo, H M.]]		[[Category: Yoo, H M.]]

OCA at 17:52, 19 June 2013

2013-06-19T17:52:35Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4g4e|  PDB=4g4e  |  SCENE=  }}
-The entry 4g4e is ON HOLD  until Paper Publication
+==Function==
-Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H.
+==About this Structure==
-Description: Crystal structure of the L88A mutant of HslV from Escherichia coli
+==Reference==

OCA at 04:57, 8 August 2012

2012-08-08T04:57:23Z

← Older revision		Revision as of 04:57, 8 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4g4e is ON HOLD		The entry 4g4e is ON HOLD until Paper Publication

	Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H.		Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H.

	Description: Crystal structure of the L88A mutant of HslV from Escherichia coli		Description: Crystal structure of the L88A mutant of HslV from Escherichia coli

OCA: Protected "4g4e" [edit=sysop:move=sysop]

2012-07-25T06:52:00Z

Protected "4g4e" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:52, 25 July 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4g4e is ON HOLD Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H. Description: Crystal str...

2012-07-25T06:51:59Z

New page: '''Unreleased structure''' The entry 4g4e is ON HOLD Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H. Description: Crystal str...

New page

'''Unreleased structure'''

The entry 4g4e is ON HOLD

Authors: Lee, J.W., Park, E, Yoo, H.M., Ha, B.H., An, J.Y., Jeon, Y.J., Seol, J.H., Eom, S.H., Chung, C.H.

Description: Crystal structure of the L88A mutant of HslV from Escherichia coli