当前位置: X-MOL 学术Nat. Commun. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis.
Nature Communications ( IF 14.7 ) Pub Date : 2020-07-07 , DOI: 10.1038/s41467-020-17202-8
Yong Zi Tan,José Rodrigues,James E Keener,Ruixiang Blake Zheng,Richard Brunton,Brian Kloss,Sabrina I Giacometti,Ana L Rosário,Lei Zhang,Michael Niederweis,Oliver B Clarke,Todd L Lowary,Michael T Marty,Margarida Archer,Clinton S Potter,Bridget Carragher,Filippo Mancia

Arabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyltransferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti-tuberculosis drug ethambutol. We present the 3.3 Å resolution single-particle cryo-electron microscopy structure of Mycobacterium smegmatis EmbB, providing insights on substrate binding and reaction mechanism. Mutations that confer ethambutol resistance map mostly around the putative active site, suggesting this to be the location of drug binding.



中文翻译:


来自耻垢分枝杆菌的阿拉伯糖基转移酶 EmbB 的冷冻电镜结构。



阿拉伯糖基转移酶 B (EmbB) 属于膜结合糖基转移酶家族,可构建分枝杆菌细胞包膜的脂化多糖,并且是抗结核药物乙胺丁醇的靶标。我们展示了耻垢分枝杆菌EmbB 的 3.3 Å 分辨率单颗粒冷冻电子显微镜结构,为底物结合和反应机制提供了见解。赋予乙胺丁醇抗性的突变主要分布在假定的活性位点周围,表明这是药物结合的位置。

更新日期:2020-07-07
down
wechat
bug