2ioq

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[[Image:2ioq.gif|left|200px]]
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{{Seed}}
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[[Image:2ioq.png|left|200px]]
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{{STRUCTURE_2ioq| PDB=2ioq | SCENE= }}
{{STRUCTURE_2ioq| PDB=2ioq | SCENE= }}
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'''Crystal Structure of full-length HTPG, the Escherichia coli HSP90'''
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===Crystal Structure of full-length HTPG, the Escherichia coli HSP90===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17055434 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17055434}}
==About this Structure==
==About this Structure==
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[[Category: Heat shock protein]]
[[Category: Heat shock protein]]
[[Category: Hsp90]]
[[Category: Hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:43:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:21:45 2008''

Revision as of 14:21, 27 July 2008

Image:2ioq.png

Template:STRUCTURE 2ioq

Crystal Structure of full-length HTPG, the Escherichia coli HSP90

Template:ABSTRACT PUBMED 17055434

About this Structure

2IOQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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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