1vzy
From Proteopedia
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|PDB= 1vzy |SIZE=350|CAPTION= <scene name='initialview01'>1vzy</scene>, resolution 1.97Å | |PDB= 1vzy |SIZE=350|CAPTION= <scene name='initialview01'>1vzy</scene>, resolution 1.97Å | ||
|SITE= <scene name='pdbsite=ZNB:Act+Binding+Site+For+Chain+A'>ZNB</scene> | |SITE= <scene name='pdbsite=ZNB:Act+Binding+Site+For+Chain+A'>ZNB</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00498 Hsp33]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzy OCA], [http://www.ebi.ac.uk/pdbsum/1vzy PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1vzy RCSB]</span> | ||
}} | }} | ||
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[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
[[Category: MCSG, Midwest Center for Structural Genomics.]] | [[Category: MCSG, Midwest Center for Structural Genomics.]] | ||
| - | + | [[Category: heat shock protein,crystal engineering,molecular chaperone,redox-active center,psi,protein structure initiative,mcsg,midwest center for structural genomic]] | |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:10:11 2008'' |
Revision as of 04:10, 26 March 2008
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| , resolution 1.97Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Domains: | Hsp33 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS HSP33
Overview
The bacterial heat shock protein Hsp33 is a redox-regulated chaperone activated by oxidative stress. In response to oxidation, four cysteines within a Zn2+ binding C-terminal domain form two disulfide bonds with concomitant release of the metal. This leads to the formation of the biologically active Hsp33 dimer. The crystal structure of the N-terminal domain of the E. coli protein has been reported, but neither the structure of the Zn2+ binding motif nor the nature of its regulatory interaction with the rest of the protein are known. Here we report the crystal structure of the full-length B. subtilis Hsp33 in the reduced form. The structure of the N-terminal, dimerization domain is similar to that of the E. coli protein, although there is no domain swapping. The Zn2+ binding domain is clearly resolved showing the details of the tetrahedral coordination of Zn2+ by four thiolates. We propose a structure-based activation pathway for Hsp33.
About this Structure
1VZY is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism., Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper DR, Graf PC, Joachimiak A, Jakob U, Derewenda ZS, Structure. 2004 Oct;12(10):1901-7. PMID:15458638
Page seeded by OCA on Wed Mar 26 06:10:11 2008
Categories: Bacillus subtilis | Single protein | Bielnicki, J. | Cooper, D R. | Dauter, Z. | Derewenda, U. | Derewenda, Z S. | Devedjiev, Y. | Janda, I K. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Heat shock protein,crystal engineering,molecular chaperone,redox-active center,psi,protein structure initiative,mcsg,midwest center for structural genomic
