1EJJ

CRYSTAL STRUCTURAL ANALYSIS OF PHOSPHOGLYCERATE MUTASE COCRYSTALLIZED WITH 3-PHOSPHOGLYCERATE

1EJJ の概要

• エントリーDOI: 10.2210/pdb1ejj/pdb
• 分子名称: PHOSPHOGLYCERATE MUTASE, MANGANESE (II) ION, 3-PHOSPHOGLYCERIC ACID, ... (4 entities in total)
• 機能のキーワード: alpha/beta-type structure, isomerase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57319.49

構造登録者

Jedrzejas, M.J.,Chander, M.,Setlow, P.,Krishnasamy, G. (登録日: 2000-03-02, 公開日: 2001-03-02, 最終更新日: 2024-02-07)

主引用文献

Jedrzejas, M.J.,Chander, M.,Setlow, P.,Krishnasamy, G.
Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus.
EMBO J., 19:1419-1431, 2000

PubMed Abstract: Bacillus stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- and 3-phosphoglyceric acid (PGA), does not require 2,3-diphosphoglyceric acid for activity. However, this enzyme does have an absolute and specific requirement for Mn(2+) ions for catalysis. Here we report the crystal structure of this enzyme complexed with 3PGA and manganese ions to 1.9 A resolution; this is the first crystal structure of a diphosphoglycerate-independent PGM to be determined. This information, plus the location of the two bound Mn(2+) ions and the 3PGA have allowed formulation of a possible catalytic mechanism for this PGM. In this mechanism Mn(2+) ions facilitate the transfer of the substrate's phosphate group to Ser62 to form a phosphoserine intermediate. In the subsequent phosphotransferase part of the reaction, the phosphate group is transferred from Ser62 to the O2 or O3 positions of the reoriented glycerate to yield the PGA product. Site-directed mutagenesis studies were used to confirm our mechanism and the involvement of specific enzyme residues in Mn(2+) binding and catalysis.

PubMed: 10747010
DOI: 10.1093/emboj/19.7.1419

実験手法

X-RAY DIFFRACTION (1.9 Å)