1sf8: Difference between revisions
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[[Image:1sf8.gif|left|200px]] | [[Image:1sf8.gif|left|200px]] | ||
'''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90''' | {{Structure | ||
|PDB= 1sf8 |SIZE=350|CAPTION= <scene name='initialview01'>1sf8</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= HTPG, B0473, C0593, Z0590, ECS0526 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SF8 is a [ | 1SF8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SF8 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15274928 15274928] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: three stranded beta sheet]] | [[Category: three stranded beta sheet]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:04:09 2008'' | ||
Revision as of 15:04, 20 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | HTPG, B0473, C0593, Z0590, ECS0526 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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