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| {{STRUCTURE_1hqy| PDB=1hqy | SCENE= }} | | {{STRUCTURE_1hqy| PDB=1hqy | SCENE= }} |
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| '''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''
| | ===Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11709174}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11709174 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11709174}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hslvu]] | | [[Category: Hslvu]] |
| [[Category: Peptidase-atpase complex]] | | [[Category: Peptidase-atpase complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:08:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:33:51 2008'' |