2c7d: Difference between revisions
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[[Image:2c7d.gif|left|200px]] | [[Image:2c7d.gif|left|200px]] | ||
'''FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM COMPLEX (EMD-1181)''' | {{Structure | ||
|PDB= 2c7d |SIZE=350|CAPTION= <scene name='initialview01'>2c7d</scene> | |||
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|LIGAND= | |||
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'''FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM COMPLEX (EMD-1181)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2C7D is a [ | 2C7D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7D OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16429154 16429154] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:49 2008'' | ||
Revision as of 14:11, 20 March 2008
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FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM COMPLEX (EMD-1181)
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.
About this Structure
2C7D is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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