3GMB

Crystal Structure of 2-Methyl-3-hydroxypyridine-5-carboxylic acid Oxygenase

3GMB の概要

• エントリーDOI: 10.2210/pdb3gmb/pdb
• 関連するPDBエントリー: 3GMC
• 分子名称: 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: flavin monooxygenase, oxidoreductase
• 由来する生物種: Mesorhizobium loti (Mesorhizobium loti)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94082.41

構造登録者

McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E. (登録日: 2009-03-13, 公開日: 2009-04-14, 最終更新日: 2024-10-30)

主引用文献

McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E.
Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications.
Biochemistry, 48:4139-4149, 2009

PubMed Abstract: A vitamin B(6) degradative pathway has recently been identified and characterized in Mesorhizobium loti MAFF303099. One of the enzymes on this pathway, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO), is a flavin-dependent enzyme and catalyzes the oxidative ring-opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid to form E-2-(acetamino-methylene)succinate. The gene for this enzyme has been cloned, and the corresponding protein has been overexpressed in Escherichia coli and purified. The crystal structure of MHPCO has been solved to 2.1 A using SAD phasing with and without the substrate MHPC bound. These crystal structures provide insight into the reaction mechanism and suggest roles for active site residues in the catalysis of a novel oxidative ring-opening reaction.

PubMed: 19317437
DOI: 10.1021/bi900149f

実験手法

X-RAY DIFFRACTION (2.1 Å)