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Structural basis for arginine glycosylation of host substrates by bacterial effector proteins

Authors
 Jun Bae Park  ;  Young Hun Kim  ;  Youngki Yoo  ;  Juyeon Kim  ;  Sung-Hoon Jun  ;  Jin Won Cho  ;  Samir El Qaidi  ;  Samuel Walpole  ;  Serena Monaco  ;  Ana A. García-García  ;  Miaomiao Wu  ;  Michael P. Hays  ;  Ramon Hurtado-Guerrero  ;  Jesus Angulo  ;  Philip R. Hardwidge  ;  Jeon-Soo Shin  ;  Hyun-Soo Cho 
Citation
 NATURE COMMUNICATIONS, Vol.9 : 4283, 2018 
Journal Title
 NATURE COMMUNICATIONS 
Issue Date
2018
Abstract
The bacterial effector proteins SseK and NleB glycosylate host proteins on arginine residues, leading to reduced NF-κB-dependent responses to infection. Salmonella SseK1 and SseK2 are E. coli NleB1 orthologs that behave as NleB1-like GTs, although they differ in protein substrate specificity. Here we report that these enzymes are retaining glycosyltransferases composed of a helix-loop-helix (HLH) domain, a lid domain, and a catalytic domain. A conserved HEN motif (His-Glu-Asn) in the active site is important for enzyme catalysis and bacterial virulence. We observe differences between SseK1 and SseK2 in interactions with substrates and identify substrate residues that are critical for enzyme recognition. Long Molecular Dynamics simulations suggest that the HLH domain determines substrate specificity and the lid-domain regulates the opening of the active site. Overall, our data suggest a front-face SNi mechanism, explain differences in activities among these effectors, and have implications for future drug development against enteric pathogens.
Files in This Item:
T201803819.pdf Download
DOI
10.1038/s41467-018-06680-6
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Shin, Jeon Soo(신전수) ORCID logo https://orcid.org/0000-0002-8294-3234
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/165304
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