Premium
Crystal structure of 5‐methylthioribose 1‐phosphate isomerase product complex from Bacillus subtilis : Implications for catalytic mechanism
Author(s) -
Tamura Haruka,
Saito Yohtaro,
Ashida Hiroki,
Inoue Tsuyoshi,
Kai Yasushi,
Yokota Akiho,
Matsumura Hiroyoshi
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073169008
Subject(s) - bacillus subtilis , active site , isomerase , chemistry , stereochemistry , nucleoside , enzyme , catalysis , biochemistry , biology , bacteria , genetics
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 Å 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.