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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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| Главные авторы: | , , , , , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2004
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| Предметы: | |
| Online-ссылка: | 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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