The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism

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...

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Veröffentlicht in:Journal of applied physics 2004-10, Vol.12 (10), p.1901-1907
Hauptverfasser: Janda, Izabela, Devedjiev, Yancho, Derewenda, Urszula, Dauter, Zbigniew, Bielnicki, Jakub, Cooper, David R, Graf, Paul C F, Joachimiak, Andrzej, Jakob, Ursula, Derewenda, Zygmunt S
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container_end_page 1907
container_issue 10
container_start_page 1901
container_title Journal of applied physics
container_volume 12
creator Janda, Izabela
Devedjiev, Yancho
Derewenda, Urszula
Dauter, Zbigniew
Bielnicki, Jakub
Cooper, David R
Graf, Paul C F
Joachimiak, Andrzej
Jakob, Ursula
Derewenda, Zygmunt S
description 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.
doi_str_mv 10.1016/j.str.2004.08.003
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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. 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ispartof Journal of applied physics, 2004-10, Vol.12 (10), p.1901-1907
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source MEDLINE; Cell Press Free Archives; AIP Journals Complete; Access via ScienceDirect (Elsevier); AIP Digital Archive; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry
subjects Amino Acid Sequence
Bacillus subtilis - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
BNL
CRYSTAL STRUCTURE
Crystallography
Dimerization
Entropy
Escherichia coli Proteins - chemistry
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
MATERIALS SCIENCE
Models, Molecular
Molecular Chaperones - chemistry
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Molecular Sequence Data
Mutagenesis
national synchrotron light source
Oxidation-Reduction
PHYSICS
Protein Structure, Tertiary - genetics
Sequence Homology, Amino Acid
Zinc - chemistry
Zinc - metabolism
title The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism
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