2gq0
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Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90
OverviewOverview
In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton, heat-shock protein (hsp90) chaperone family facilitate the folding and, conformational changes of a broad array of proteins important in cell, signaling, proliferation, and survival. Here we describe the effects of, nucleotides on the structure of full-length HtpG, the Escherichia coli, hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations., Structural characterization of nucleotide-free and ADP bound HtpG was, extended to higher resolution by X-ray crystallography. In the absence of, nucleotide, HtpG exhibits an "open" conformation in which the three, domains of each monomer present hydrophobic elements into the large cleft, formed by the dimer. By contrast, ADP binding drives dramatic, conformational changes that allow these hydrophobic elements to converge, and shield each other from solvent, suggesting a mechanism by which, nucleotides could control client protein binding and release.
About this StructureAbout this Structure
2GQ0 is a Single protein structure of sequence from Escherichia coli. Active as Non-chaperonin molecular chaperone ATPase, with EC number 3.6.4.10 Full crystallographic information is available from OCA.
ReferenceReference
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements., Shiau AK, Harris SF, Southworth DR, Agard DA, Cell. 2006 Oct 20;127(2):329-40. PMID:17055434
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