1sf8: Difference between revisions
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|PDB= 1sf8 |SIZE=350|CAPTION= <scene name='initialview01'>1sf8</scene>, resolution 2.60Å | |PDB= 1sf8 |SIZE=350|CAPTION= <scene name='initialview01'>1sf8</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |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> | ||
|ACTIVITY= | |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]) | |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= | |||
|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> | |||
}} | }} | ||
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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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:41:15 2008'' | ||
Revision as of 23:41, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | HTPG, B0473, C0593, Z0590, ECS0526 (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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