5ji2 - Revision history

OCA at 18:52, 20 September 2023

2023-09-20T18:52:49Z

←Older revision		Revision as of 18:52, 20 September 2023
Line 3:		Line 3:
	<StructureSection load='5ji2' size='340' side='right'caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>		<StructureSection load='5ji2' size='340' side='right'caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Eco55 Eco55~~] and [~~http~~://en.wikipedia.org/wiki/~~Eco57 Eco57~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_55989 Escherichia coli 55989] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.307Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4a\|1g4a]]~~, [[~~5ji3~~\|~~5ji3~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>hslV, EC55989_4410 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~585055 ECO55]), hslU, htpI, Z5478, ECs4858 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=5ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji2 OCA], [https://pdbe.org/5ji2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ji2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ji2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji2 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=5ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji2 OCA], [~~http~~://pdbe.org/5ji2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ji2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ji2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji2 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HSLV_ECO55 HSLV_ECO55]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. [[http://www.uniprot.org/uniprot/HSLU_ECO57 HSLU_ECO57]] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	+	[https://www.uniprot.org/uniprot/HSLV_ECO55 HSLV_ECO55] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Eco55~~]]	+	[[Category: Escherichia coli 55989]]
-	[[Category: ~~Eco57]]~~	+	[[Category: Escherichia coli O157:H7]]
-	~~[[Category~~: ~~HslU--HslV peptidase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baytshtok, V]]	+	[[Category: Baytshtok V]]
-	[[Category: Grant~~, R A~~]]	+	[[Category: Grant RA]]
-	[[Category: Sauer~~, R T~~]]	+	[[Category: Sauer RT]]
-	[[Category: Schmitz~~, K R]]~~	+	[[Category: Schmitz KR]]
-	~~[[Category: Aaa+ atpase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Peptidase~~]]	+

OCA at 16:22, 11 December 2019

2019-12-11T16:22:43Z

←Older revision		Revision as of 16:22, 11 December 2019
Line 1:		Line 1:

	==HslU L199Q in HslUV complex==		==HslU L199Q in HslUV complex==
-	<StructureSection load='5ji2' size='340' side='right' caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>	+	<StructureSection load='5ji2' size='340' side='right'caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco55 Eco55] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco55 Eco55] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[ATPase\|ATPase]]	+	*[[ATPase 3D structures\|ATPase 3D structures]]
-	*[[Heat Shock ~~Proteins~~\|Heat Shock ~~Proteins~~]]	+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 32:
	[[Category: Eco57]]		[[Category: Eco57]]
	[[Category: HslU--HslV peptidase]]		[[Category: HslU--HslV peptidase]]
		+	[[Category: Large Structures]]
	[[Category: Baytshtok, V]]		[[Category: Baytshtok, V]]
	[[Category: Grant, R A]]		[[Category: Grant, R A]]

OCA at 05:48, 25 April 2018

2018-04-25T05:48:25Z

←Older revision		Revision as of 05:48, 25 April 2018
Line 14:		Line 14:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	~~BACKGROUND:~~ The ~~bacterial heat shock locus~~ HslU ~~ATPase~~ and ~~HslV peptidase together form an ATP-dependent HslVU protease. Bacterial HslVU is~~ a ~~homolog of~~ the ~~eukaryotic 26S proteasome. Crystallographic studies of HslVU should provide an understanding of ATP-dependent~~ protein ~~unfolding~~, ~~translocation~~, and ~~proteolysis by this and other ATP~~-~~dependent proteases. RESULTS: We present~~ a ~~3.0 A resolution crystal structure~~ of ~~HslVU with an~~ HslU ~~hexamer bound at one end of an HslV dodecamer~~. The structure ~~shows that the central pores~~ of the ~~ATPase and peptidase are next~~ to ~~each other and aligned~~. ~~The central pore~~ of ~~HslU consists of a GYVG motif~~, ~~which is conserved among protease-associated ATPases. The binding~~ of ~~one HslU hexamer to one end~~ of ~~an HslV dodecamer in the 3.0 A resolution structure opens both HslV central pores~~ and ~~induces asymmetric~~ changes ~~in HslV. CONCLUSIONS: Analysis~~ of ~~nucleotide binding induced conformational changes in~~ the ~~current and previous HslU structures suggests a protein unfolding-coupled translocation mechanism~~. ~~In this mechanism~~, ~~unfolded polypeptides are threaded through the aligned pores~~ of the ~~ATPase and peptidase and translocated into the peptidase central chamber~~.	+	The I domain of HslU sits above the AAA+ ring and forms a funnel-like entry to the axial pore, where protein substrates are engaged, unfolded, and translocated into HslV for degradation. The L199Q I-domain substitution, which was originally reported as a loss-of-function mutation, resides in a segment that appears to adopt multiple conformations as electron density is not observed in HslU and HslUV crystal structures. The L199Q sequence change does not alter the structure of the AAA+ ring or its interactions with HslV but increases I-domain susceptibility to limited endoproteolysis. Notably, the L199Q mutation increases the rate of ATP hydrolysis substantially, results in slower degradation of some proteins but faster degradation of other substrates, and markedly changes the preference of HslUV for initiating degradation at the N or C terminus of model substrates. Thus, a structurally dynamic region of the I domain plays a key role in controlling protein degradation by HslUV.

-	~~Crystal structures~~ of the ~~HslVU peptidase-ATPase complex reveal an~~ ATP~~-dependent proteolysis mechanism~~.,~~Wang J~~, ~~Song JJ~~, ~~Franklin MC~~, ~~Kamtekar S~~, ~~Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH~~ Structure. ~~2001 Feb 7~~;9(2):~~177~~-84. PMID:~~11250202~~<ref>PMID:~~11250202~~</ref>	+	A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.,Baytshtok V, Fei X, Grant RA, Baker TA, Sauer RT Structure. 2016 Oct 4;24(10):1766-1777. doi: 10.1016/j.str.2016.08.012. Epub 2016, Sep 22. PMID:27667691<ref>PMID:27667691</ref>

	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 5ji2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5ji2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase\|ATPase]]
		+	*[[Heat Shock Proteins\|Heat Shock Proteins]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:57, 15 November 2017

2017-11-15T17:57:59Z

←Older revision		Revision as of 17:57, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='5ji2' size='340' side='right' caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>		<StructureSection load='5ji2' size='340' side='right' caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco55 Eco55] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4a\|1g4a]], [[5ji3\|5ji3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4a\|1g4a]], [[5ji3\|5ji3]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hslV, EC55989_4410 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585055 ECO55]), hslU, htpI, Z5478, ECs4858 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=5ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji2 OCA], [http://pdbe.org/5ji2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ji2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ji2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji2 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=5ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji2 OCA], [http://pdbe.org/5ji2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ji2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ji2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji2 ProSAT]</span></td></tr>
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Eco55]]
		+	[[Category: Eco57]]
	[[Category: HslU--HslV peptidase]]		[[Category: HslU--HslV peptidase]]
	[[Category: Baytshtok, V]]		[[Category: Baytshtok, V]]

OCA at 18:35, 10 December 2016

2016-12-10T18:35:35Z

←Older revision		Revision as of 18:35, 10 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5ji2 is ~~ON HOLD until Paper~~ Publication	+	==HslU L199Q in HslUV complex==
		+	<StructureSection load='5ji2' size='340' side='right' caption='[[5ji2]], [[Resolution\|resolution]] 3.31Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5ji2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JI2 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4a\|1g4a]], [[5ji3\|5ji3]]</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=5ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ji2 OCA], [http://pdbe.org/5ji2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ji2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ji2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ji2 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HSLV_ECO55 HSLV_ECO55]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. [[http://www.uniprot.org/uniprot/HSLU_ECO57 HSLU_ECO57]] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: The bacterial heat shock locus HslU ATPase and HslV peptidase together form an ATP-dependent HslVU protease. Bacterial HslVU is a homolog of the eukaryotic 26S proteasome. Crystallographic studies of HslVU should provide an understanding of ATP-dependent protein unfolding, translocation, and proteolysis by this and other ATP-dependent proteases. RESULTS: We present a 3.0 A resolution crystal structure of HslVU with an HslU hexamer bound at one end of an HslV dodecamer. The structure shows that the central pores of the ATPase and peptidase are next to each other and aligned. The central pore of HslU consists of a GYVG motif, which is conserved among protease-associated ATPases. The binding of one HslU hexamer to one end of an HslV dodecamer in the 3.0 A resolution structure opens both HslV central pores and induces asymmetric changes in HslV. CONCLUSIONS: Analysis of nucleotide binding induced conformational changes in the current and previous HslU structures suggests a protein unfolding-coupled translocation mechanism. In this mechanism, unfolded polypeptides are threaded through the aligned pores of the ATPase and peptidase and translocated into the peptidase central chamber.

-	~~Authors: Grant, R.A~~., ~~Sauer~~, ~~R.T.~~, ~~Schmitz~~, ~~K.R.~~, ~~Baytshtok~~, V.	+	Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism.,Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH Structure. 2001 Feb 7;9(2):177-84. PMID:11250202<ref>PMID:11250202</ref>

-	~~Description: HslU L199Q in HslUV complex~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category: Schmitz~~, K.~~R]]~~	+	<div class="pdbe-citations 5ji2" style="background-color:#fffaf0;"></div>
-	~~[[Category~~: ~~Sauer, R.T]]~~	+	== References ==
-	[[Category: ~~Grant, R.A~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: HslU--HslV peptidase]]
	[[Category: Baytshtok, V]]		[[Category: Baytshtok, V]]
		+	[[Category: Grant, R A]]
		+	[[Category: Sauer, R T]]
		+	[[Category: Schmitz, K R]]
		+	[[Category: Aaa+ atpase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Peptidase]]

OCA: Protected "5ji2" [edit=sysop:move=sysop]

2016-05-11T02:06:07Z

Protected "5ji2" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:06, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5ji2 is ON HOLD until Paper Publication Authors: Grant, R.A., Sauer, R.T., Schmitz, K.R., Baytshtok, V. Description: HslU L199Q in HslUV complex [[...

2016-05-11T02:06:05Z

New page: '''Unreleased structure''' The entry 5ji2 is ON HOLD until Paper Publication Authors: Grant, R.A., Sauer, R.T., Schmitz, K.R., Baytshtok, V. Description: HslU L199Q in HslUV complex [[...

New page

'''Unreleased structure'''

The entry 5ji2 is ON HOLD until Paper Publication

Authors: Grant, R.A., Sauer, R.T., Schmitz, K.R., Baytshtok, V.

Description: HslU L199Q in HslUV complex
[[Category: Unreleased Structures]]
[[Category: Schmitz, K.R]]
[[Category: Sauer, R.T]]
[[Category: Grant, R.A]]
[[Category: Baytshtok, V]]