Verification of the interdomain contact site in the inactive monomer, and the domain‐swapped fold in the active dimer of Hsp33 in solution

FEBS Letters - Tập 586 - Trang 411-415 - 2012
Yoo-Sup Lee1, Kyoung-Seok Ryu2, Seo-Jin Kim1, Hyun-Suk Ko1, Dae-Won Sim1, Young Ho Jeon3, Eun-Hee Kim2, Wahn-Soo Choi4, Hyung-Sik Won1
1Department of Biotechnology, Research Institute for Biomedical & Health Science, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea
2Division of Magnetic Resonance, Korea Basic Science Institute, Ochang, Chungbuk 363-883, Republic of Korea
3College of Pharmacy, Korea University Jochiwon, Chungnam 339-700, Republic of Korea
4Department of Immunology, College of Medicine, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea

Tóm tắt

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.

Tài liệu tham khảo

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Thông tin xuất bản

FEBS Letters

Tập 586

411-415

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