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Verification of the interdomain contact site in the inactive monomer, and the domain‐swapped fold in the active dimer of Hsp33 in solution
Author(s) -
Lee Yoo-Sup,
Ryu Kyoung-Seok,
Kim Seo-Jin,
Ko Hyun-Suk,
Sim Dae-Won,
Jeon Young Ho,
Kim Eun-Hee,
Choi Wahn-Soo,
Won Hyung-Sik
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.01.011
Subject(s) - dimer , chemistry , crystallography , monomer , active site , crystal structure , quenching (fluorescence) , chaperone (clinical) , biophysics , fluorescence , biology , biochemistry , catalysis , physics , polymer , medicine , organic chemistry , pathology , quantum mechanics
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.