1sf8
From Proteopedia
(New page: 200px<br /><applet load="1sf8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sf8, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1sf8.gif|left|200px]]<br /><applet load="1sf8" size=" | + | [[Image:1sf8.gif|left|200px]]<br /><applet load="1sf8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sf8, resolution 2.60Å" /> | caption="1sf8, resolution 2.60Å" /> | ||
'''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90'''<br /> | '''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hsp90 is a ubiquitous, well-conserved molecular chaperone involved in the | + | Hsp90 is a ubiquitous, well-conserved molecular chaperone involved in the folding and stabilization of diverse proteins. Beyond its capacity for general protein folding, Hsp90 influences a wide array of cellular signaling pathways that underlie key biological and disease processes. It has been proposed that Hsp90 functions as a molecular clamp, dimerizing through its carboxy-terminal domain and utilizing ATP binding and hydrolysis to drive large conformational changes including transient dimerization of the amino-terminal and middle domains. We have determined the 2.6 A X-ray crystal structure of the carboxy-terminal domain of htpG, the Escherichia coli Hsp90. This structure reveals a novel fold and that dimerization is dependent upon the formation of a four-helix bundle. Remarkably, proximal to the helical dimerization motif, each monomer projects a short helix into solvent. The location, flexibility, and amphipathic character of this helix suggests that it may play a role in substrate binding and hence chaperone activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1SF8 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 NI and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SF8 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=NI:'>NI</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SF8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Agard, D | + | [[Category: Agard, D A.]] |
| - | [[Category: Harris, S | + | [[Category: Harris, S F.]] |
| - | [[Category: Shiau, A | + | [[Category: Shiau, A K.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: NI]] | [[Category: NI]] | ||
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[[Category: three stranded beta sheet]] | [[Category: three stranded beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:52 2008'' |
Revision as of 13:00, 21 February 2008
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Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90
Overview
Hsp90 is a ubiquitous, well-conserved molecular chaperone involved in the folding and stabilization of diverse proteins. Beyond its capacity for general protein folding, Hsp90 influences a wide array of cellular signaling pathways that underlie key biological and disease processes. It has been proposed that Hsp90 functions as a molecular clamp, dimerizing through its carboxy-terminal domain and utilizing ATP binding and hydrolysis to drive large conformational changes including transient dimerization of the amino-terminal and middle domains. We have determined the 2.6 A X-ray crystal structure of the carboxy-terminal domain of htpG, the Escherichia coli Hsp90. This structure reveals a novel fold and that dimerization is dependent upon the formation of a four-helix bundle. Remarkably, proximal to the helical dimerization motif, each monomer projects a short helix into solvent. The location, flexibility, and amphipathic character of this helix suggests that it may play a role in substrate binding and hence chaperone activity.
About this Structure
1SF8 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site., Harris SF, Shiau AK, Agard DA, Structure. 2004 Jun;12(6):1087-97. PMID:15274928
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