1sf8
From Proteopedia
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| - | [[Image:1sf8.gif|left|200px]] | + | [[Image:1sf8.gif|left|200px]] |
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| - | '''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 12:04, 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
Overview
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 Structure
1SF8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:15274928
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