title: Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.
abstract: The crystal structure of alanine racemase from Oenococcus oeni has been determined at 1.7 Å resolution using the single-wavelength anomalous dispersion (SAD) method and selenium-labelled protein. The protein exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites. Pyridoxal 5'-phosphate, a cofactor, is bound to each monomer and forms a Schiff base with Lys39. Structural comparison of alanine racemase from O. oeni (Alr) with homologous family members revealed similar domain organization and cofactor binding.
authors.affiliation: Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
authors.forename: Kandavelu
authors.initials: K
authors.lastname: Palani
authors.forename: Stephen K
authors.initials: SK
authors.lastname: Burley
authors.forename: Subramanyam
authors.initials: S
authors.lastname: Swaminathan
mesh_terms: D000411:Alanine Racemase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D056585:Oenococcus / Q000201:enzymology*; D011487:Protein Conformation; D017510:Protein Folding; D055503:Protein Multimerization; D011732:Pyridoxal Phosphate / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D011732:Pyridoxal Phosphate; D000411:Alanine Racemase