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Title: Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate. Author: Palani K, Burley SK, Swaminathan S. Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Jan 01; 69(Pt 1):15-9. PubMed ID: 23295479. 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.[Abstract] [Full Text] [Related] [New Search]