变形链球菌D-丙氨酸：D-丙氨酸连接酶（DDl）脱辅基形式的晶体结构

Crystal structure of the Apo form of D-Alanine:D-Alanine ligase (DDl) from Streptococcus mutans.

作者信息

Lu Yongzhi, Xu Hongyan, Zhao Xiaojun

机构信息

West China Hospital Nanomedicine Laboratory, Center for Regenerative Medicine and Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital Sichuan University, Chengdu 610065, Sichuan, China.

出版信息

Protein Pept Lett. 2010 Aug;17(8):1053-7. doi: 10.2174/092986610791498858.

DOI:10.2174/092986610791498858

PMID:20522004

Abstract

D-Alanine:D-Alanine ligase (DDl) catalyzes the formation of D-Alanine:D-Alanine dipeptide and is an essential enzyme in bacterial cell wall biosynthesis.. This enzyme does not have a human ortholog, making it an attractive target for developing new antibiotic drugs. We determined the crystal structure at 2.23 A resolution of DDl from Streptococcus mutans (SmDDl), the principal aetiological agent of human dental caries. This structure reveals that SmDDl is a dimer and has a disordered omega-loop region.

摘要

D-丙氨酸：D-丙氨酸连接酶（DDl）催化D-丙氨酸：D-丙氨酸二肽的形成，是细菌细胞壁生物合成中的一种必需酶。该酶在人类中没有直系同源物，这使其成为开发新型抗生素药物的一个有吸引力的靶点。我们确定了变形链球菌（SmDDl）中DDl在2.23埃分辨率下的晶体结构，变形链球菌是人类龋齿的主要病原体。该结构表明SmDDl是一种二聚体，并且有一个无序的ω-环区域。