1gr5

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{{STRUCTURE_1gr5| PDB=1gr5 | SCENE= }}
{{STRUCTURE_1gr5| PDB=1gr5 | SCENE= }}
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'''SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY'''
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===SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY===
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==Overview==
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The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
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(as it appears on PubMed at http://www.pubmed.gov), where 11779463 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11779463}}
==About this Structure==
==About this Structure==
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[[Category: Chaperonin]]
[[Category: Chaperonin]]
[[Category: Hsp60 class]]
[[Category: Hsp60 class]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:55:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:56:27 2008''

Revision as of 02:56, 1 July 2008

Image:1gr5.png

Template:STRUCTURE 1gr5

SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY

Template:ABSTRACT PUBMED 11779463

About this Structure

1GR5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

ATP-bound states of GroEL captured by cryo-electron microscopy., Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR, Cell. 2001 Dec 28;107(7):869-79. PMID:11779463

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