Open AccessStructure of alanine racemase from Oenococcus oeni with bound pyridoxal 5′‐phosphate
Author(s) -
Palani Kandavelu,
Burley Stephen K.,
Swaminathan Subramanyam
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112047276
Subject(s) - oenococcus oeni , pyridoxal 5 phosphate , alanine , chemistry , pyridoxal phosphate , phosphate , pyridoxal , biochemistry , amino acid , biology , enzyme , malolactic fermentation , cofactor , genetics , bacteria , lactic acid
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.