title: Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.
abstract: Upon dimerization by oxidation, Hsp33 functions as a molecular chaperone in prokaryotes. Previously published structures of both the inactive and active species are of doubtful relevance to the solution conformations since the inactive (reduced) crystal structure was dimeric, while the active (oxidized) species was crystallized with a truncation of its regulation domain. The interdomain contact site of the inactive monomer, identified in this work, is consistent with that previously observed in the reduced dimer crystal. In contrast, fluorescence quenching of the active dimer contradicted the results expected from the domain-swapped fold observed in the truncated dimer crystal. The results of this study provide important new information concerning controversial issues in the activation process of Hsp33.
authors.affiliation: Department of Biotechnology, Research Institute for Biomedical & Health Science, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk, Republic of Korea.
authors.forename: Yoo-Sup
authors.initials: YS
authors.lastname: Lee
authors.forename: Kyoung-Seok
authors.initials: KS
authors.lastname: Ryu
authors.forename: Seo-Jin
authors.initials: SJ
authors.lastname: Kim
authors.forename: Hyun-Suk
authors.initials: HS
authors.lastname: Ko
authors.forename: Dae-Won
authors.initials: DW
authors.lastname: Sim
authors.forename: Young Ho
authors.initials: YH
authors.lastname: Jeon
authors.forename: Eun-Hee
authors.initials: EH
authors.lastname: Kim
authors.forename: Wahn-Soo
authors.initials: WS
authors.lastname: Choi
authors.forename: Hyung-Sik
authors.initials: HS
authors.lastname: Won
mesh_terms: D019281:Dimerization; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012996:Solutions; D013050:Spectrometry, Fluorescence
chemical_list: D029968:Escherichia coli Proteins; C492165:HSP33 protein, E coli; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; D012996:Solutions