1sf8: Difference between revisions

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[[Image:1sf8.gif|left|200px]]
[[Image:1sf8.gif|left|200px]]


{{Structure
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|PDB= 1sf8 |SIZE=350|CAPTION= <scene name='initialview01'>1sf8</scene>, resolution 2.60&Aring;
The line below this paragraph, containing "STRUCTURE_1sf8", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>
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|ACTIVITY=
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|GENE= HTPG, B0473, C0593, Z0590, ECS0526 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
-->
|DOMAIN=
{{STRUCTURE_1sf8| PDB=1sf8 |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sf8 OCA], [http://www.ebi.ac.uk/pdbsum/1sf8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sf8 RCSB]</span>
}}


'''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90'''
'''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90'''
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[[Category: Harris, S F.]]
[[Category: Harris, S F.]]
[[Category: Shiau, A K.]]
[[Category: Shiau, A K.]]
[[Category: exposed amphipathic helix]]
[[Category: Exposed amphipathic helix]]
[[Category: four helix bundle dimerization interface]]
[[Category: Four helix bundle dimerization interface]]
[[Category: three stranded beta sheet]]
[[Category: Three stranded beta sheet]]
 
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Revision as of 08:37, 3 May 2008

File:1sf8.gif

Template:STRUCTURE 1sf8

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


OverviewOverview

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.

About this StructureAbout this Structure

1SF8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site., Harris SF, Shiau AK, Agard DA, Structure. 2004 Jun;12(6):1087-97. PMID:15274928 Page seeded by OCA on Sat May 3 08:37:44 2008

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