3PIM

Crystal structure of Mxr1 from Saccharomyces cerevisiae in unusual oxidized form

Summary for 3PIM

• Entry DOI: 10.2210/pdb3pim/pdb
• Related: 3PIL 3PIN
• Descriptor: Peptide methionine sulfoxide reductase (2 entities in total)
• Functional Keywords: methionine-s-sulfoxide reductase, oxidoreductase
• Biological source: Saccharomyces cerevisiae (yeast)
• Total number of polymer chains: 3
• Total formula weight: 64533.57

Authors

Ma, X.X.,Guo, P.C.,Shi, W.W.,Luo, M.,Tan, X.F.,Chen, Y.,Zhou, C.Z. (deposition date: 2010-11-07, release date: 2011-02-23, Last modification date: 2024-11-20)

Primary citation

Ma, X.X.,Guo, P.C.,Shi, W.W.,Luo, M.,Tan, X.F.,Chen, Y.,Zhou, C.Z.
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1
J.Biol.Chem., 286:13430-13437, 2011

PubMed Abstract: 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 Å, 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.

PubMed: 21345799
DOI: 10.1074/jbc.M110.205161

Experimental method

X-RAY DIFFRACTION (1.9 Å)