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Crystal structure of maize serine racemase with pyridoxal 5′-phosphate.
- Source :
-
Acta Crystallographica: Section F, Structural Biology Communications . Mar2016, Vol. 72 Issue 3, p165-171. 6p. - Publication Year :
- 2016
-
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]
- Subjects :
- *RACEMASES
*VITAMIN B6
*PROTEIN crystallography
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 72
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 113444943
- Full Text :
- https://doi.org/10.1107/S2053230X16000960