PDBsum entry 4xpl

Transferase

PDB id: 4xpl

Contents

Protein chain

141 a.a.

Ligands

ACO

Waters ×77

PDB id:

4xpl

Name:

Transferase

Title:

The crystal structure of campylobacter jejuni n-acetyltransferase pseh in complex with acetyl coenzyme a

Structure:

N-acetyltransferase, pseh. Chain: a. Engineered: yes. Mutation: yes

Source:

Campylobacter jejuni subsp. Jejuni pt14. Organism_taxid: 1201032. Gene: a911_06385. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.95Å R-factor: 0.190 R-free: 0.229

Authors:

W.S.Song,M.S.Nam,B.Namgung,S.I.Yoon

Key ref:

W.S.Song et al. (2015). Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation. Biochem Biophys Res Commun, 458, 843-848. PubMed id: 25698400 DOI: 10.1016/j.bbrc.2015.02.041

Date:

17-Jan-15 Release date: 18-Mar-15

Protein chain

A0A0J9X276  (A0A0J9X276_CAMJU) -  N-Acetyltransferase, PseH from Campylobacter jejuni subsp. jejuni PT14

Seq: 163 a.a.

Struc: 141 a.a.

DOI no: 10.1016/j.bbrc.2015.02.041

Biochem Biophys Res Commun 458:843-848 (2015)

PubMed id: 25698400

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

W.S.Song, M.S.Nam, B.Namgung, S.I.Yoon.

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.