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Crystal structure of maize serine racemase with pyridoxal 5'-phosphate.

ABSTRACT: Serine racemase (SR) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesis in vivo. The first X-ray crystal structure of maize SR was determined to 2.1 Å resolution and PLP binding was confirmed in solution by UV-Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat and fission yeast SRs reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix.

SUBMITTER: Zou L

PROVIDER: S-EPMC4774874 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Crystal structure of maize serine racemase with pyridoxal 5'-phosphate.

Zou Lingling L Song Yang Y Wang Chengliang C Sun Jiaqi J Wang Leilei L Cheng Beijiu B Fan Jun J

Acta crystallographica. Section F, Structural biology communications 20160216 Pt 3

Serine racemase (SR) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesis in vivo. The first X-ray crystal structure of maize SR was determined to 2.1 Å resolution and PLP binding was confirmed in solution by UV-Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat ...[more]

PMID: 26919519

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