3GMB

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

Summary for 3GMB

• Entry DOI: 10.2210/pdb3gmb/pdb
• Related: 3GMC
• Descriptor: 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: flavin monooxygenase, oxidoreductase
• Biological source: Mesorhizobium loti (Mesorhizobium loti)
• Total number of polymer chains: 2
• Total formula weight: 94082.41

Authors

McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E. (deposition date: 2009-03-13, release date: 2009-04-14, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)