1xck

OverviewOverview

The 2.9A resolution crystal structure of apo wild-type GroEL was, determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed, in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the, mutations as well as to the presence of a crystallographic symmetry, the, ring-ring interface was inaccurately described. Analysis of the present, structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission., We also show unambiguously that there is no ATP-induced 102 degrees, rotation of the apical domain helix I around its helical axis, as, previously assumed in the crystal structure of the (GroEL-KMgATP)(14), complex, and analyze the apical domain movements. These results enabled us, to compare our structure with other GroEL crystal structures already, published, allowing us to suggest a new route through which the allosteric, signal for negative cooperativity propagates within the molecule. The, proposed mechanism, supported by known mutagenesis data, underlines the, importance of the switching of salt bridges.

About this StructureAbout this Structure

1XCK is a Single protein structure of sequence from Escherichia coli with SO4, K, MPD and PEG as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915

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