1ksf
From Proteopedia
(New page: 200px<br /><applet load="1ksf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ksf, resolution 2.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ksf.gif|left|200px]]<br /><applet load="1ksf" size=" | + | [[Image:1ksf.gif|left|200px]]<br /><applet load="1ksf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ksf, resolution 2.60Å" /> | caption="1ksf, resolution 2.60Å" /> | ||
'''Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains'''<br /> | '''Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component | + | Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1KSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, MET, PGE, ADP and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=MET:'>MET</scene>, <scene name='pdbligand=PGE:'>PGE</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Esser, L.]] | [[Category: Esser, L.]] | ||
[[Category: Guo, F.]] | [[Category: Guo, F.]] | ||
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
[[Category: Xia, D.]] | [[Category: Xia, D.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: crystal structure]] | [[Category: crystal structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:25 2008'' |
Revision as of 11:37, 21 February 2008
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Crystal Structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease: Structural basis of differences in Function of the Two AAA+ ATPase domains
Overview
Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component of the ATP-dependent ClpAP protease, participates in regulatory protein degradation and the dissolution and degradation of protein aggregates. The crystal structure of the ClpA subunit reveals an N-terminal domain with pseudo-twofold symmetry and two AAA(+) modules (D1 and D2) each consisting of a large and a small sub-domain with ADP bound in the sub-domain junction. The N-terminal domain interacts with the D1 domain in a manner similar to adaptor-binding domains of other AAA(+) proteins. D1 and D2 are connected head-to-tail consistent with a cooperative and vectorial translocation of protein substrates. In a planar hexamer model of ClpA, built by assembling ClpA D1 and D2 into homohexameric rings of known structures of AAA(+) modules, the differences in D1-D1 and D2-D2 interfaces correlate with their respective contributions to hexamer stability and ATPase activity.
About this Structure
1KSF is a Single protein structure of sequence from Escherichia coli with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease., Guo F, Maurizi MR, Esser L, Xia D, J Biol Chem. 2002 Nov 29;277(48):46743-52. Epub 2002 Aug 29. PMID:12205096
Page seeded by OCA on Thu Feb 21 13:37:25 2008
Categories: Escherichia coli | Single protein | Esser, L. | Guo, F. | Maurizi, M R. | Xia, D. | ADP | IPA | MET | MG | PGE | Aaa+ | Atp-dependent protease | Atpases | Chaperones | Clpa | Crystal structure
