Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5′‐phosphate. Issue 1 (8th January 2013)

• Record Type: Journal Article
• Authors: Palani, Kandavelu; Burley, Stephen K.; Swaminathan, Subramanyam
• Is Part Of: Acta crystallographica. Volume 69:Issue 1(2013:Jan.)
• Page Start: 15
• Page End: 19
• Publication Date: 2013-01-08
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309112047276
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The crystal structure of alanine racemase from <italic>Oenococcus oeni</italic> 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 <italic>O. oeni</italic> (Alr) with homologous family members revealed similar domain organization and cofactor binding.</p> </abstract>