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Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslUNucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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