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1hqy
From Proteopedia
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Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU
Overview
BACKGROUND: The bacterial heat shock locus ATPase HslU is an AAA(+), protein that has structures known in many nucleotide-free and -bound, states. Nucleotide is required for the formation of the biologically, active HslU hexameric assembly. The hexameric HslU ATPase binds the, dodecameric HslV peptidase and forms an ATP-dependent HslVU protease., RESULTS: We have characterized four distinct HslU conformational states, going sequentially from open to closed: the empty, SO(4), ATP, and ADP, states. The nucleotide binds at a cleft formed by an alpha/beta domain and, an alpha-helical domain in HslU. The four HslU states differ by a rotation, of the alpha-helical domain. This classification leads to a correction of, nucleotide identity in one structure and reveals the ATP, hydrolysis-dependent structural changes in the HslVU complex, including a, ring rotation and a conformational change of the HslU C terminus. This, leads to an amended protein unfolding-coupled translocation mechanism., CONCLUSIONS: The observed nucleotide-dependent conformational changes in, HslU and their governing principles provide a framework for the, mechanistic understanding of other AAA(+) proteins.
About this Structure
1HQY is a Protein complex structure of sequences from Escherichia coli with ADP as ligand. Full crystallographic information is available from OCA.
Reference
Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU., Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, Eom SH, Chung CH, Structure. 2001 Nov;9(11):1107-16. PMID:11709174
Page seeded by OCA on Tue Nov 20 16:45:52 2007
