research communications
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.
Keywords: structural comparison; serine racemase; maize; crystal structure; cofactor; pyridoxal 5'-phosphate.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X16000960/no5092sup1.pdf |
PDB reference: maize serine racemase, complex with PLP, 5cvc