2c7e: Difference between revisions

Revision as of 08:58, 28 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:2c7e.png

Template:STRUCTURE 2c7e

REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)

Template:ABSTRACT PUBMED 11779463

About this StructureAbout this Structure

2C7E is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1gr6. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 08:58:21 2008

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

OCA

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 {{STRUCTURE_2c7e|  PDB=2c7e  |  SCENE=  }}
-'''REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)'''
+===REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11779463}}, adds the Publication Abstract to the page
+(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==
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 [[Category: Nucleotide-binding]]
 [[Category: Phosphorylation]]
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