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Structure of alanine racemase from

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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.
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Document Type: Research Article

Publication date: January 1, 2013

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