1k6k

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[[Image:1k6k.jpg|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1ksf|1KSF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6k OCA], [http://www.ebi.ac.uk/pdbsum/1k6k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k6k RCSB]</span>
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'''Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains'''
'''Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains'''
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[[Category: Maurizi, M R.]]
[[Category: Maurizi, M R.]]
[[Category: Xia, D.]]
[[Category: Xia, D.]]
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[[Category: adaptor binding]]
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[[Category: Adaptor binding]]
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[[Category: atpase]]
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[[Category: Atpase]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: clpa]]
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[[Category: Clpa]]
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[[Category: n-domain]]
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[[Category: N-domain]]
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[[Category: structure]]
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[[Category: Structure]]
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[[Category: x-ray]]
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Revision as of 19:22, 2 May 2008

Image:1k6k.jpg

Template:STRUCTURE 1k6k

Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two 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

1K6K 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 Page seeded by OCA on Fri May 2 22:22:06 2008

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