This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5ioa

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:41, 26 July 2016

Chaperone Spy bound to Im7 (Im7 un-modeled)

Structural highlights

5ioa is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	5ina, 5ioe, 5iog
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Quan S, Koldewey P, Tapley T, Kirsch N, Ruane KM, Pfizenmaier J, Shi R, Hofmann S, Foit L, Ren G, Jakob U, Xu Z, Cygler M, Bardwell JC. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol. 2011 Feb 13. PMID:21317898 doi:10.1038/nsmb.2016
↑ Quan S, Wang L, Petrotchenko EV, Makepeace KA, Horowitz S, Yang J, Zhang Y, Borchers CH, Bardwell JC. Super Spy variants implicate flexibility in chaperone action. Elife. 2014;3:e01584. doi: 10.7554/eLife.01584. Epub 2014 Feb 4. PMID:24497545 doi:http://dx.doi.org/10.7554/eLife.01584
↑ Stull F, Koldewey P, Humes JR, Radford SE, Bardwell JC. Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nat Struct Mol Biol. 2016 Jan;23(1):53-8. doi: 10.1038/nsmb.3133. Epub 2015 Nov, 30. PMID:26619265 doi:http://dx.doi.org/10.1038/nsmb.3133
↑ 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. Visualizing chaperone-assisted protein folding. Nat Struct Mol Biol. 2016 May 30. doi: 10.1038/nsmb.3237. PMID:27239796 doi:http://dx.doi.org/10.1038/nsmb.3237

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ioa"

Categories: Bardwell, J C.A | Horowitz, S | Koldewey, P | Martin, R | Chaperone

@@ Line 6: / Line 6: @@
 </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]], [[5ioe|5ioe]], [[5iog|5iog]]</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=5ioa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ioa OCA], [http://pdbe.org/5ioa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ioa RCSB], [http://www.ebi.ac.uk/pdbsum/5ioa 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=5ioa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ioa OCA], [http://pdbe.org/5ioa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ioa RCSB], [http://www.ebi.ac.uk/pdbsum/5ioa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ioa ProSAT]</span></td></tr>
 </table>
 == Function ==

5ioa

From Proteopedia

Revision as of 06:41, 26 July 2016

Chaperone Spy bound to Im7 (Im7 un-modeled)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox