1. Crystal structure of maize serine racemase with pyridoxal 5′-phosphate.
- Author
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Zou, Lingling, Sun, Jiaqi, Wang, Leilei, Cheng, Beijiu, Fan, Jun, Song, Yang, and Wang, Chengliang
- Subjects
RACEMASES ,VITAMIN B6 ,PROTEIN crystallography - 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. [ABSTRACT FROM AUTHOR]
- Published
- 2016
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