Structural basis for arginine glycosylation of host substrates by bacterial effector proteins
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 viv...
| Main Authors: | , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-06680-6 |
| _version_ | 1831773679533424640 |
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| author | 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 |
| author_facet | 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 |
| author_sort | Jun Bae Park |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T08:42:08Z |
| format | Article |
| id | doaj.art-49a452b7d1ba4b249efc0b07a970adb6 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-22T08:42:08Z |
| publishDate | 2018-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-49a452b7d1ba4b249efc0b07a970adb62022-12-21T18:32:13ZengNature PortfolioNature Communications2041-17232018-10-019111510.1038/s41467-018-06680-6Structural basis for arginine glycosylation of host substrates by bacterial effector proteinsJun Bae Park0Young Hun Kim1Youngki Yoo2Juyeon Kim3Sung-Hoon Jun4Jin Won Cho5Samir El Qaidi6Samuel Walpole7Serena Monaco8Ana A. García-García9Miaomiao Wu10Michael P. Hays11Ramon Hurtado-Guerrero12Jesus Angulo13Philip R. Hardwidge14Jeon-Soo Shin15Hyun-Soo Cho16Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guDepartment of Microbiology, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-guDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guCollege of Veterinary Medicine, Kansas State UniversitySchool of Pharmacy, University of East Anglia, Norwich Research ParkSchool of Pharmacy, University of East Anglia, Norwich Research ParkBIFI, University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+DCollege of Veterinary Medicine, Kansas State UniversityCollege of Veterinary Medicine, Kansas State UniversityBIFI, University of Zaragoza, BIFI-IQFR (CSIC) Joint Unit, Mariano Esquillor s/n, Campus Rio Ebro, Edificio I+DSchool of Pharmacy, University of East Anglia, Norwich Research ParkCollege of Veterinary Medicine, Kansas State UniversityDepartment of Microbiology, Yonsei University College of Medicine, 50-1 Yonsei-ro, Seodaemun-guDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-guThe 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.https://doi.org/10.1038/s41467-018-06680-6 |
| spellingShingle | 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 Structural basis for arginine glycosylation of host substrates by bacterial effector proteins Nature Communications |
| title | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| title_full | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| title_fullStr | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| title_full_unstemmed | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| title_short | Structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| title_sort | structural basis for arginine glycosylation of host substrates by bacterial effector proteins |
| url | https://doi.org/10.1038/s41467-018-06680-6 |
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