1K6K

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

Summary for 1K6K

• Entry DOI: 10.2210/pdb1k6k/pdb
• Related: 1KSF
• Descriptor: ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA (2 entities in total)
• Functional Keywords: clpa, chaperone, atpase, adaptor binding, n-domain, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 16200.27

Authors

Guo, F.,Maurizi, M.R.,Esser, L.,Xia, D. (deposition date: 2001-10-16, release date: 2002-09-27, Last modification date: 2024-04-03)

Primary citation

Guo, F.,Maurizi, M.R.,Esser, L.,Xia, D.
Crystal structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease
J.Biol.Chem., 277:46743-46752, 2002

PubMed Abstract: 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.

PubMed: 12205096
DOI: 10.1074/jbc.M207796200

Experimental method

X-RAY DIFFRACTION (1.8 Å)