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http://purl.uniprot.org/citations/15458638http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15458638http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.08.003"xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Dauter Z."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Joachimiak A."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Cooper D.R."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Derewenda U."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Derewenda Z.S."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Devedjiev Y."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Jakob U."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Janda I."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Bielnicki J."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/author"Graf P.C."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/pages"1901-1907"xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/title"The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism."xsd:string
http://purl.uniprot.org/citations/15458638http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/15458638http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15458638
http://purl.uniprot.org/citations/15458638http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15458638
http://purl.uniprot.org/uniprot/#_P37565-mappedCitation-15458638http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15458638
http://purl.uniprot.org/uniprot/P37565http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15458638