2YRF

Crystal structure of 5-methylthioribose 1-phosphate isomerase from Bacillus subtilis complexed with sulfate ion

2YRF の概要

• エントリーDOI: 10.2210/pdb2yrf/pdb
• 分子名称: Methylthioribose-1-phosphate isomerase, SULFATE ION (3 entities in total)
• 機能のキーワード: isomerase, methionine salvage pathway
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82603.60

構造登録者

Tamura, H.,Inoue, T.,Kai, Y.,Matsumura, H. (登録日: 2007-04-02, 公開日: 2008-01-22, 最終更新日: 2024-10-30)

主引用文献

Tamura, H.,Saito, Y.,Ashida, H.,Inoue, T.,Kai, Y.,Yokota, A.,Matsumura, H.
Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: Implications for catalytic mechanism
Protein Sci., 17:126-135, 2008

PubMed Abstract: The methionine salvage pathway (MSP) plays a crucial role in recycling a sulphahydryl derivative of the nucleoside. Recently, the genes and reactions in MSP from Bacillus subtilis have been identified, where 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). Herein, we report the crystal structures of B. subtilis M1Pi (Bs-M1Pi) in complex with its product MTRu-1-P, and a sulfate at 2.4 and 2.7 A resolution, respectively. The electron density clearly shows the presence of each compound in the active site. The structural comparison with other homologous proteins explains how the substrate uptake of Bs-M1Pi may be induced by an open/closed transition of the active site. The highly conserved residues at the active site, namely, Cys160 and Asp240 are most likely to be involved in catalysis. The structural analysis sheds light on its catalytic mechanism of M1Pi.

PubMed: 18156470
DOI: 10.1110/ps.073169008

実験手法

X-RAY DIFFRACTION (2.7 Å)