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윤성일 교수 (시스템면역과학과)

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작성자 : 의생명과학대학 날짜 : 작성일15-04-30 11:28 조회 : 931회

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

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-b-L-altrosamine to produce UDP-2,4-diacetamido-2,4,6-trideoxy-b-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
b-sheet decorated by four a-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.

,Biochemical and Biophysical Research Communications 458 (2015) 843-848
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