Harris, SF, Shiau, AK and Agard, DA (2004) The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12:1087-97
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.
Adenosine Triphosphate/chemistry; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Dimerization; Dose-Response Relationship, Drug; Escherichia coli/metabolism; Escherichia coli Proteins; HSP90 Heat-Shock Proteins/chemistry; Hydrolysis; Kinetics; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid
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