2c7c: Difference between revisions

Revision as of 19:07, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2c7c.png

Template:STRUCTURE 2c7c

FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)

Template:ABSTRACT PUBMED 16429154

About this StructureAbout this Structure

2C7C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes., Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR, Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154

Page seeded by OCA on Sun Jul 27 19:07:19 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2c7c.gif|left|200px]]
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 {{STRUCTURE_2c7c|  PDB=2c7c  |  SCENE=  }}
-'''FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)'''
+===FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)===
-==Overview==
+<!--
-The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_16429154}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16429154 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16429154}}
 ==About this Structure==
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 [[Category: Nucleotide-binding]]
 [[Category: Phosphorylation]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:07:19 2008''