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现在位置:首页 > 科研进展 > 最新重要论文(影响因子PNAS及以上)
Structural and Functional Insights into Host Death Domains Inactivation by the Bacterial Arginine GlcNAcyltransferase Effector, Mol Cell, 09 Apr 2019
2019-04-09 | 【     】【打印】【关闭

Molecular Cell, 09 April, 2019, DOI: https://doi.org/10.1016/j.molcel.2019.03.028

Structural and Functional Insights into Host Death Domains Inactivation by the Bacterial Arginine GlcNAcyltransferase Effector

Jingjin Ding, Xing Pan, Lijie Du, Qing Yao, Juan Xue, Hongwei Yao, Da-Cheng Wang, Shan Li, Feng Shao

Summary

Enteropathogenic E. coli NleB and related type III effectors catalyze arginine GlcNAcylation of death domain (DD) proteins to block host defense, but the underlying mechanism is unknown. Here we solve crystal structures of NleB alone and in complex with FADD-DD, UDP, and Mn2+ as well as NleB-GlcNAcylated DDs of TRADD and RIPK1. NleB adopts a GT-A fold with a unique helix-pair insertion to hold FADD-DD; the interface contacts explain the selectivity of NleB for certain DDs. The acceptor arginine is fixed into a cleft, in which Glu253 serves as a base to activate the guanidinium. Analyses of the enzyme-substrate complex and the product structures reveal an inverting sugar-transfer reaction and a detailed catalytic mechanism. These structural insights are validated by mutagenesis analyses of NleB-mediated GlcNAcylation in vitro and its function in mouse infection. Our study builds a structural framework for understanding of NleB-catalyzed arginine GlcNAcylation of host death domain.

文章链接:https://www.cell.com/molecular-cell/fulltext/S1097-2765(19)30232-1

相关报道:http://www.dztrb.tw/kyjz/zxdt/201904/t20190410_5272485.html

 

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