Structural highlights
Function
[MSRA_YEAST] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product.
Publication Abstract from PubMed
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 A, 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.
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.,Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ J Biol Chem. 2011 Apr 15;286(15):13430-7. Epub 2011 Feb 23. PMID:21345799[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ. Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1. J Biol Chem. 2011 Apr 15;286(15):13430-7. Epub 2011 Feb 23. PMID:21345799 doi:http://dx.doi.org/10.1074/jbc.M110.205161
