2011年4月15日，我室生物大分子结构与功能研究部周丛照教授研究组在JOURNAL OF BIOLOGICAL CHEMISTRY上发表题为Structural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1的论文。

Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 286 Issue: 15 Pages: 13430-13437 Published: APR 15 2011
Ma XX (Ma, Xiao-Xiao)1, Guo PC (Guo, Peng-Chao)1, Shi WW (Shi, Wei-Wei)1, Luo M (Luo, Ming)1, Tan XF (Tan, Xiao-Feng)1, Chen YX (Chen, Yuxing)1, Zhou CZ (Zhou, Cong-Zhao)1
Addresses:
1. Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Anhui Peoples R China
E-mail Addresses: zcz@ustc.edu.cn

Reprint Address: Zhou, CZ (reprint author), Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Anhui Peoples R China

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 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.