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

Acta Crystallogr F Struct Biol Commun. 2016 Mar;72(Pt 3):165-71. doi: 10.1107/S2053230X16000960. Epub 2016 Feb 16.

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.

Keywords: cofactor; crystal structure; maize; pyridoxal 5′-phosphate; serine racemase; structural comparison.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain
  • Conserved Sequence
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Models, Molecular
  • Plant Proteins / chemistry*
  • Protein Conformation, alpha-Helical
  • Protein Structure, Quaternary
  • Pyridoxal Phosphate / chemistry
  • Racemases and Epimerases
  • Structural Homology, Protein
  • Zea mays / enzymology*

Substances

  • Plant Proteins
  • Pyridoxal Phosphate
  • Racemases and Epimerases
  • serine racemase