1hqy: Difference between revisions
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[[Image:1hqy.gif|left|200px]]<br /><applet load="1hqy" size=" | [[Image:1hqy.gif|left|200px]]<br /><applet load="1hqy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hqy, resolution 2.80Å" /> | caption="1hqy, resolution 2.80Å" /> | ||
'''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''<br /> | '''Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: The bacterial heat shock locus ATPase HslU is an AAA(+) | 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== | ==About this Structure== | ||
1HQY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1HQY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Chung, C | [[Category: Chung, C H.]] | ||
[[Category: Eom, S | [[Category: Eom, S H.]] | ||
[[Category: Franklin, M | [[Category: Franklin, M C.]] | ||
[[Category: Kamtekar, S.]] | [[Category: Kamtekar, S.]] | ||
[[Category: Seong, I | [[Category: Seong, I S.]] | ||
[[Category: Song, J | [[Category: Song, J J.]] | ||
[[Category: Wang, J.]] | [[Category: Wang, J.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: peptidase-atpase complex]] | [[Category: peptidase-atpase complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:06 2008'' | ||
Revision as of 11:04, 21 February 2008
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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 with ADP as ligand. 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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