The Crystal Structure of the Reduced, Zn(2+)-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 Zn(2+) binding C-terminal domain form two disulfide bonds with concomitant release of the metal. This leads to the formation of the biologically acti...

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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.
Format: Artigo
Sprache:Inglês
Veröffentlicht: 2004
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Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3691021/
https://ncbi.nlm.nih.gov/pubmed/15458638
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2004.08.003
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