1gr5
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gr5 OCA], [http://www.ebi.ac.uk/pdbsum/1gr5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gr5 RCSB]</span> | ||
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[[Category: hsp60 class]] | [[Category: hsp60 class]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:46 2008'' |
Revision as of 17:49, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY
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
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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