1hqy: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1e94|1E94]], [[1doo|1DOO]], [[1g4a|1G4A]], [[1g4b|1G4B]], [[1g3i|1G3I]], [[1ht1|1HT1]], [[1ht2|1HT2]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqy OCA], [http://www.ebi.ac.uk/pdbsum/1hqy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hqy RCSB]</span> | |||
}} | }} | ||
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[[Category: Song, J J.]] | [[Category: Song, J J.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: hslvu]] | [[Category: hslvu]] | ||
[[Category: peptidase-atpase complex]] | [[Category: peptidase-atpase complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:15 2008'' | ||
Revision as of 21:09, 30 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Related: | 1E94, 1DOO, 1G4A, 1G4B, 1G3I, 1HT1, 1HT2
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU
OverviewOverview
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 StructureAbout this Structure
1HQY is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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