5iog - Revision history

OCA: Redirecting to 5wo2

OCA — Fri, 06 Oct 2017 05:34:33 GMT

Redirecting to 5wo2

←Older revision		Revision as of 05:34, 6 October 2017
Line 1:		Line 1:
-		+	#REDIRECT [[5wo2]] This PDB entry is obsolete and replaced by 5wo2
-	~~==Chaperone Spy bound to Casein Fragment (Casein un-modeled)==~~	+
-	~~<StructureSection load='5iog' size='340' side='right' caption='~~[[~~5iog]], [[Resolution\|resolution]] 1.77Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[5iog~~]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IOG FirstGlance]. <br>	+
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ina\|5ina]], [[5ioa\|5ioa]], [[5ioe\|5ioe]]</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=5iog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iog OCA], [http://pdbe.org/5iog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iog RCSB], [http://www.ebi.ac.uk/pdbsum/5iog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iog ProSAT]</span></td></tr>	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	~~[[http://www.uniprot.org/uniprot/SPY_ECOLI SPY_ECOLI]] An ATP-independent periplasmic chaperone, decreases protein aggregation~~ and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref> <ref>PMID:24497545</ref> <ref>PMID:26619265</ref>	+
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding. Obtaining structural ensembles of chaperone-substrate complexes would ultimately reveal how chaperones help proteins fold into their native state. To address this problem, we devised a new structural biology approach based on X-ray crystallography, termed residual electron and anomalous density (READ). READ enabled us to visualize even sparsely populated conformations of the substrate protein immunity protein 7 (Im7) in complex with the Escherichia coli chaperone Spy, and to capture a series of snapshots depicting the various folding states of Im7 bound to Spy. The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone.	+
-		+
-	Visualizing chaperone-assisted protein folding.,Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL 3rd, Bardwell JC Nat Struct Mol Biol. 2016 May 30. doi: 10.1038/nsmb.3237. PMID:27239796<ref>PMID:27239796</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5iog" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Bardwell, J C.A]]~~	+
-	~~[[Category: Horowitz, S]]~~	+
-	~~[[Category: Koldewey, P]]~~	+
-	~~[[Category: Martin, R]]~~	+
-	~~[[Category: Chaperone]]~~	+

OCA at 06:20, 26 July 2016

OCA — Tue, 26 Jul 2016 06:20:39 GMT

←Older revision		Revision as of 06:20, 26 July 2016
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ina\|5ina]], [[5ioa\|5ioa]], [[5ioe\|5ioe]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ina\|5ina]], [[5ioa\|5ioa]], [[5ioe\|5ioe]]</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=5iog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iog OCA], [http://pdbe.org/5iog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iog RCSB], [http://www.ebi.ac.uk/pdbsum/5iog 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=5iog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iog OCA], [http://pdbe.org/5iog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iog RCSB], [http://www.ebi.ac.uk/pdbsum/5iog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iog ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:28, 20 June 2016

OCA — Mon, 20 Jun 2016 07:28:05 GMT

←Older revision		Revision as of 07:28, 20 June 2016
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SPY_ECOLI SPY_ECOLI]] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref> <ref>PMID:24497545</ref> <ref>PMID:26619265</ref>		[[http://www.uniprot.org/uniprot/SPY_ECOLI SPY_ECOLI]] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref> <ref>PMID:24497545</ref> <ref>PMID:26619265</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding. Obtaining structural ensembles of chaperone-substrate complexes would ultimately reveal how chaperones help proteins fold into their native state. To address this problem, we devised a new structural biology approach based on X-ray crystallography, termed residual electron and anomalous density (READ). READ enabled us to visualize even sparsely populated conformations of the substrate protein immunity protein 7 (Im7) in complex with the Escherichia coli chaperone Spy, and to capture a series of snapshots depicting the various folding states of Im7 bound to Spy. The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone.
		+
		+	Visualizing chaperone-assisted protein folding.,Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL 3rd, Bardwell JC Nat Struct Mol Biol. 2016 May 30. doi: 10.1038/nsmb.3237. PMID:27239796<ref>PMID:27239796</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5iog" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:10, 2 June 2016

OCA — Thu, 02 Jun 2016 06:10:31 GMT

←Older revision		Revision as of 06:10, 2 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5iog is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Chaperone Spy bound to Casein Fragment (Casein un-modeled)==
-		+	<StructureSection load='5iog' size='340' side='right' caption='[[5iog]], [[Resolution\|resolution]] 1.77Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5iog]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IOG FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ina\|5ina]], [[5ioa\|5ioa]], [[5ioe\|5ioe]]</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=5iog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iog OCA], [http://pdbe.org/5iog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iog RCSB], [http://www.ebi.ac.uk/pdbsum/5iog PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPY_ECOLI SPY_ECOLI]] An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).<ref>PMID:21317898</ref> <ref>PMID:24497545</ref> <ref>PMID:26619265</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bardwell, J C.A]]
		+	[[Category: Horowitz, S]]
		+	[[Category: Koldewey, P]]
		+	[[Category: Martin, R]]
		+	[[Category: Chaperone]]

OCA at 14:35, 15 May 2016

OCA — Sun, 15 May 2016 14:35:50 GMT

←Older revision		Revision as of 14:35, 15 May 2016
Line 3:		Line 3:
	The entry 5iog is ON HOLD until Paper Publication		The entry 5iog is ON HOLD until Paper Publication

-	Authors: ~~Horowitz, S., Koldewey, P., Martin, R., Bardwell, J.C.A.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Bardwell, J.C.A]]
-	[[Category: Koldewey, P]]
-	[[Category: Horowitz, S]]
-	[[Category: Martin, R]]

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

OCA — Wed, 11 May 2016 00:43:11 GMT

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

←Older revision

Revision as of 00:43, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5iog is ON HOLD until Paper Publication Authors: Horowitz, S., Koldewey, P., Martin, R., Bardwell, J.C.A. Description: [[Category: Unreleased Stru...

OCA — Wed, 11 May 2016 00:43:09 GMT

New page: '''Unreleased structure''' The entry 5iog is ON HOLD until Paper Publication Authors: Horowitz, S., Koldewey, P., Martin, R., Bardwell, J.C.A. Description: [[Category: Unreleased Stru...

New page

'''Unreleased structure'''

The entry 5iog is ON HOLD until Paper Publication

Authors: Horowitz, S., Koldewey, P., Martin, R., Bardwell, J.C.A.

Description:
[[Category: Unreleased Structures]]
[[Category: Bardwell, J.C.A]]
[[Category: Koldewey, P]]
[[Category: Horowitz, S]]
[[Category: Martin, R]]