1SF8

Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90

Summary for 1SF8

• Entry DOI: 10.2210/pdb1sf8/pdb
• Descriptor: Chaperone protein htpG, NICKEL (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: four helix bundle dimerization interface, exposed amphipathic helix, three stranded beta sheet, chaperone
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6Z3
• Total number of polymer chains: 8
• Total formula weight: 116290.93

Authors

Harris, S.F.,Shiau, A.K.,Agard, D.A. (deposition date: 2004-02-19, release date: 2004-06-15, Last modification date: 2024-10-30)

Primary citation

Harris, S.F.,Shiau, A.K.,Agard, D.A.
The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.
Structure, 12:1087-1097, 2004

PubMed Abstract: 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.

PubMed: 15274928
DOI: 10.1016/j.str.2004.03.020

Experimental method

X-RAY DIFFRACTION (2.6 Å)