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

被引：6

作者：

Zou, Lingling ^{[1
]}

Song, Yang ^{[2
]}

Wang, Chengliang ^{[2
]}

Sun, Jiaqi ^{[1
]}

Wang, Leilei ^{[1
]}

Cheng, Beijiu ^{[1
]}

Fan, Jun ^{[1
]}

机构：

[1] Anhui Agr Univ, Sch Life Sci, Hefei 230036, Anhui, Peoples R China

[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Anhui, Peoples R China

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2016年 / 72卷

关键词：

structural comparison; serine racemase; maize; crystal structure; cofactor; pyridoxal 5 '-phosphate; GENE; BINDING; ATP;

D O I：

10.1107/S2053230X16000960

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom 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.

引用

页码：165 / 171

页数：7

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