2ior

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|PDB= 2ior |SIZE=350|CAPTION= <scene name='initialview01'>2ior</scene>, resolution 1.65&Aring;
|PDB= 2ior |SIZE=350|CAPTION= <scene name='initialview01'>2ior</scene>, resolution 1.65&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= htpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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[[Category: hsp90]]
[[Category: hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:32:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:21:53 2008''

Revision as of 13:21, 23 March 2008

Image:2ior.gif


PDB ID 2ior

Drag the structure with the mouse to rotate
, resolution 1.65Å
Ligands: , and
Gene: htpG (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the N-terminal Domain of HtpG, the Escherichia coli Hsp90, Bound to ADP


Overview

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 Structure

2IOR 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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