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

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.
PDB ID: 3GMBDownload
MMDB ID: 70860
PDB Deposition Date: 2009/3/13
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3GMB: dimeric; determined by author
Molecular Components in 3GMB
Label Count Molecule
Proteins (2 molecules)
2-methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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