1ksf

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spinqualitylabelsall models PDB ID 1ksf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.60Å
Ligands:	, , , and
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains

Overview

Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.

About this Structure

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

Reference

Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease., Guo F, Maurizi MR, Esser L, Xia D, J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:12205096

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