Crystal structure of maize serine racemase with pyridoxal 5′-phosphate
详细信息 查看全文
- 作者：Lingling Zou ; Yang Song ; Chengliang Wang ; Jiaqi Sun ; Leilei Wang ; Beijiu Cheng and Jun Fan
- 关键词：structural comparison ; serine racemase ; maize ; crystal structure ; cofactor ; pyridoxal 5&prime ; -phosphate
- 刊名：Acta Crystallographica Section F
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：72
- 期：3
- 页码：165-171
- 全文大小：1772K
- ISSN：1744-3091
文摘
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.