Nature Communications (Oct 2018)
Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
- 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
Affiliations
- Jun Bae Park
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- Young Hun Kim
- Department of Microbiology, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu
- Youngki Yoo
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- Juyeon Kim
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- Sung-Hoon Jun
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- Jin Won Cho
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- Samir El Qaidi
- College of Veterinary Medicine, Kansas State University
- Samuel Walpole
- School of Pharmacy, University of East Anglia, Norwich Research Park
- Serena Monaco
- School of Pharmacy, University of East Anglia, Norwich Research Park
- Ana A. García-García
- BIFI, University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D
- Miaomiao Wu
- College of Veterinary Medicine, Kansas State University
- Michael P. Hays
- College of Veterinary Medicine, Kansas State University
- Ramon Hurtado-Guerrero
- BIFI, University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+D
- Jesus Angulo
- School of Pharmacy, University of East Anglia, Norwich Research Park
- Philip R. Hardwidge
- College of Veterinary Medicine, Kansas State University
- Jeon-Soo Shin
- Department of Microbiology, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-gu
- Hyun-Soo Cho
- Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu
- DOI
- https://doi.org/10.1038/s41467-018-06680-6
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 15
Abstract
The type III secretion system effectors NleB and SseK are glycosyltransferases (GT) that specifically glycosylate arginine residues. Here the authors provide insights into their mechanism by combining X-ray crystallography, NMR, enzyme kinetics measurements, molecular dynamics simulations and in vivo experiments and show that SseK/NleB enzymes are retaining GTs.
