1hqy
From Proteopedia
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| - | [[Image:1hqy.gif|left|200px]] | + | [[Image:1hqy.gif|left|200px]] |
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| - | '''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU''' | + | {{Structure |
| + | |PDB= 1hqy |SIZE=350|CAPTION= <scene name='initialview01'>1hqy</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HQY is a [ | + | 1HQY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11709174 11709174] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptidase-atpase complex]] | [[Category: peptidase-atpase complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:31 2008'' |
Revision as of 09:40, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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