2c7e

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Revision as of 06:54, 21 November 2007

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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.

About this Structure

2C7E is a Single protein structure of sequence from Escherichia coli with K, MG and ATP as ligands. This structure superseeds the now removed PDB entry 1GR6. 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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