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- Title
Crystal structure of maize serine racemase with pyridoxal 5′-phosphate.
- Authors
Zou, Lingling; Sun, Jiaqi; Wang, Leilei; Cheng, Beijiu; Fan, Jun; Song, Yang; Wang, Chengliang
- 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.
- Subjects
RACEMASES; VITAMIN B6; PROTEIN crystallography
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2016, Vol 72, Issue 3, p165
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X16000960