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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.

SUBMITTER: Palani K

PROVIDER: S-EPMC3539696 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.

Palani Kandavelu K Burley Stephen K SK Swaminathan Subramanyam S

Acta crystallographica. Section F, Structural biology and crystallization communications 20121225 Pt 1

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 r ...[more]

PMID: 23295479

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