Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry
- Authors
- Lee, Kitaik; Yeo, Kwon Joo; Choi, Sae Hae; Lee, Eun Hye; Kim, Bo Keun; Kim, Sulhee; Cheong, Hae-Kap; Lee, Won-Kyu; Kim, Hwa-Young; Hwang, Eunha; Woo, Ju Rang; Lee, Sung-Joon; Hwang, Kwang Yeon
- Issue Date
- 11월-2020
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- domain swapping; oxidoreductases; disulfide bonds; glutaredoxin
- Citation
- IUCRJ, v.7, pp.1019 - 1027
- Indexed
- SCIE
SCOPUS
- Journal Title
- IUCRJ
- Volume
- 7
- Start Page
- 1019
- End Page
- 1027
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/51884
- DOI
- 10.1107/S2052252520011598
- ISSN
- 2052-2525
- Abstract
- Protein dimerization or oligomerization resulting from swapping part of the protein between neighboring polypeptide chains is known to play a key role in the regulation of protein function and in the formation of protein aggregates. Glutaredoxin-1 from Clostridium oremlandii (cGrx1) was used as a model to explore the formation of multiple domain-swapped conformations, which were made possible by modulating several hinge-loop residues that can form a pivot for domain swapping. Specifically, two alternative domain-swapped structures were generated and analyzed using nuclear magnetic resonance (NMR), X-ray crystallography, circular-dichroism spectroscopy and hydrogen/deuterium-exchange (HDX) mass spectrometry. The first domain-swapped structure (beta 3-swap) was formed by the hexameric cGrx1-cMsrA complex. The second domain-swapped structure (beta 1-swap) was formed by monothiol cGrx1 (C16S) alone. In summary, the first domain-swapped structure of an oxidoreductase in a hetero-oligomeric complex is presented. In particular, a single point mutation of a key cysteine residue to serine led to the formation of an intramolecular disulfide bond, as opposed to an intermolecular disulfide bond, and resulted in modulation of the underlying free-energy landscape of protein oligomerization.
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Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
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