4XPL

The crystal structure of Campylobacter jejuni N-acetyltransferase PseH in complex with acetyl coenzyme A

Summary for 4XPL

• Entry DOI: 10.2210/pdb4xpl/pdb
• Related: 4XPK
• Descriptor: N-Acetyltransferase, PseH, ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: campylobacter jejuni, pseh, bacterial glycosylation, n-acetyltransferase, transferase
• Biological source: Campylobacter jejuni subsp. jejuni PT14
• Total number of polymer chains: 1
• Total formula weight: 20188.94

Authors

Song, W.S.,Nam, M.S.,Namgung, B.,Yoon, S.I. (deposition date: 2015-01-17, release date: 2015-03-18, Last modification date: 2023-11-08)

Primary citation

Song, W.S.,Nam, M.S.,Namgung, B.,Yoon, S.I.
Structural analysis of PseH, the Campylobacter jejuni N-acetyltransferase involved in bacterial O-linked glycosylation.
Biochem.Biophys.Res.Commun., 458:843-848, 2015

PubMed 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.

PubMed: 25698400
DOI: 10.1016/j.bbrc.2015.02.041

Experimental method

X-RAY DIFFRACTION (1.95 Å)