3INT

Structure of UDP-galactopyranose mutase bound to UDP-galactose (reduced)

3INT の概要

• エントリーDOI: 10.2210/pdb3int/pdb
• 関連するPDBエントリー: 1I8T 1V0J 1WAM 2BI7 2BI8 3GF4 3INR
• 分子名称: Probable UDP-galactopyranose mutase, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: flavoenzyme, protein-ligand complex, carbohydrate biosynthesis, isomerase, fad, flavoprotein, lipopolysaccharide biosynthesis
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93021.48

構造登録者

Gruber, T.D.,Kiessling, L.L.,Forest, K.T. (登録日: 2009-08-12, 公開日: 2009-09-22, 最終更新日: 2023-09-06)

主引用文献

Gruber, T.D.,Westler, W.M.,Kiessling, L.L.,Forest, K.T.
X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin .
Biochemistry, 48:9171-9173, 2009

PubMed Abstract: The flavoenzyme uridine 5'-diphosphate galactopyranose mutase (UGM or Glf) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. The latter is a key building block for cell wall construction in numerous pathogens, including Mycobacterium tuberculosis. Mechanistic studies of UGM suggested a novel role for the flavin, and we previously provided evidence that the catalytic mechanism proceeds through a covalent flavin-galactose iminium. Here, we describe 2.3 and 2.5 A resolution X-ray crystal structures of the substrate-bound enzyme in oxidized and reduced forms, respectively. In the latter, C1 of the substrate is 3.6 A from the nucleophilic flavin N5 position. This orientation is consistent with covalent catalysis by flavin.

PubMed: 19719175
DOI: 10.1021/bi901437v

実験手法

X-RAY DIFFRACTION (2.51 Å)