1sf8
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(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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Revision as of 00:13, 21 November 2007
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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 NI and CL 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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