skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation

Abstract

Campylobacter jejuni is a bacterium that uses flagella for motility and causes worldwide acute gastroenteritis in humans. The C. jejuni N-acetyltransferase PseH (cjPseH) is responsible for the third step in flagellin O-linked glycosylation and plays a key role in flagellar formation and motility. cjPseH transfers an acetyl group from an acetyl donor, acetyl coenzyme A (AcCoA), to the amino group of UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine to produce UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose. To elucidate the catalytic mechanism of cjPseH, crystal structures of cjPseH alone and in complex with AcCoA were determined at 1.95 Å resolution. cjPseH folds into a single-domain structure of a central β-sheet decorated by four α-helices with two continuously connected grooves. A deep groove (groove-A) accommodates the AcCoA molecule. Interestingly, the acetyl end of AcCoA points toward an open space in a neighboring shallow groove (groove-S), which is occupied by extra electron density that potentially serves as a pseudosubstrate, suggesting that the groove-S may provide a substrate-binding site. Structure-based comparative analysis suggests that cjPseH utilizes a unique catalytic mechanism of acetylation that has not been observed in other glycosylation-associated acetyltransferases. Thus, our studies on cjPseH will provide valuable information for the design of new antibiotics to treat C. jejuni-induced gastroenteritis. - Highlights: • cjPseH adopts a single-domainmore » structure of a central β-sheet decorated by α-helices. • cjPseH features two continuously connected grooves on the protein surface. • Acetyl coenzyme A (AcCoA) binds into a deep groove of cjPseH in an ‘L’ shape. • The acetyl end of AcCoA points to a wide groove, a potential substrate-binding site.« less

Authors:
; ;  [1];  [1];  [2]
  1. Department of Systems Immunology, College of Biomedical Science, Kangwon National University, Chuncheon 200-701 (Korea, Republic of)
  2. (Korea, Republic of)
Publication Date:
OSTI Identifier:
22458540
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 458; Journal Issue: 4; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ACETYLATION; ANTIBIOTICS; BACTERIA; COENZYMES; CRYSTAL STRUCTURE; DOMAIN STRUCTURE; ELECTRON DENSITY; HUMAN POPULATIONS; PROTEINS; RESOLUTION; SHAPE; SHEETS; SURFACES

Citation Formats

Song, Wan Seok, Nam, Mi Sun, Namgung, Byeol, Yoon, Sung-il, E-mail: sungil@kangwon.ac.kr, and Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 200-701. Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation. United States: N. p., 2015. Web. doi:10.1016/J.BBRC.2015.02.041.
Song, Wan Seok, Nam, Mi Sun, Namgung, Byeol, Yoon, Sung-il, E-mail: sungil@kangwon.ac.kr, & Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 200-701. Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation. United States. doi:10.1016/J.BBRC.2015.02.041.
Song, Wan Seok, Nam, Mi Sun, Namgung, Byeol, Yoon, Sung-il, E-mail: sungil@kangwon.ac.kr, and Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 200-701. Fri . "Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation". United States. doi:10.1016/J.BBRC.2015.02.041.
@article{osti_22458540,
title = {Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation},
author = {Song, Wan Seok and Nam, Mi Sun and Namgung, Byeol and Yoon, Sung-il, E-mail: sungil@kangwon.ac.kr and Institute of Bioscience and Biotechnology, Kangwon National University, Chuncheon 200-701},
abstractNote = {Campylobacter jejuni is a bacterium that uses flagella for motility and causes worldwide acute gastroenteritis in humans. The C. jejuni N-acetyltransferase PseH (cjPseH) is responsible for the third step in flagellin O-linked glycosylation and plays a key role in flagellar formation and motility. cjPseH transfers an acetyl group from an acetyl donor, acetyl coenzyme A (AcCoA), to the amino group of UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine to produce UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose. To elucidate the catalytic mechanism of cjPseH, crystal structures of cjPseH alone and in complex with AcCoA were determined at 1.95 Å resolution. cjPseH folds into a single-domain structure of a central β-sheet decorated by four α-helices with two continuously connected grooves. A deep groove (groove-A) accommodates the AcCoA molecule. Interestingly, the acetyl end of AcCoA points toward an open space in a neighboring shallow groove (groove-S), which is occupied by extra electron density that potentially serves as a pseudosubstrate, suggesting that the groove-S may provide a substrate-binding site. Structure-based comparative analysis suggests that cjPseH utilizes a unique catalytic mechanism of acetylation that has not been observed in other glycosylation-associated acetyltransferases. Thus, our studies on cjPseH will provide valuable information for the design of new antibiotics to treat C. jejuni-induced gastroenteritis. - Highlights: • cjPseH adopts a single-domain structure of a central β-sheet decorated by α-helices. • cjPseH features two continuously connected grooves on the protein surface. • Acetyl coenzyme A (AcCoA) binds into a deep groove of cjPseH in an ‘L’ shape. • The acetyl end of AcCoA points to a wide groove, a potential substrate-binding site.},
doi = {10.1016/J.BBRC.2015.02.041},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 458,
place = {United States},
year = {Fri Mar 20 00:00:00 EDT 2015},
month = {Fri Mar 20 00:00:00 EDT 2015}
}