1ht2: Difference between revisions

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[[Image:1ht2.gif|left|200px]]
{{Seed}}
[[Image:1ht2.png|left|200px]]


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{{STRUCTURE_1ht2|  PDB=1ht2  |  SCENE=  }}  
{{STRUCTURE_1ht2|  PDB=1ht2  |  SCENE=  }}  


'''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''
===Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU===




==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}}


==About this Structure==
==About this Structure==
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[[Category: Hslvu]]
[[Category: Hslvu]]
[[Category: Peptidase-atpase complex]]
[[Category: Peptidase-atpase complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:38:25 2008''

Revision as of 05:38, 1 July 2008

File:1ht2.png

Template:STRUCTURE 1ht2

Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU

Template:ABSTRACT PUBMED 11709174

About this Structure

1HT2 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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