Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 15, Pages 13430-13437Publisher
ELSEVIER
DOI: 10.1074/jbc.M110.205161
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Funding
- National Natural Science Foundation of China [30870490]
- Ministry of Science and Technology of China [2006CB910202]
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The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 angstrom, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic cushion to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.
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