Abstract
Alanine racemase from
O. oeni
exists as a dimer in the crystal structure. Both monomers contribute to the two active sites present, one for each monomer.
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.