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

Biochemical and Biophysical Research Communications

Volumn 458, Issue 4, 2015, Pages 843-848

  Song, Wan Seok ^a   Nam, Mi Sun ^a   Namgung, Byeol ^a   Yoon, Sung Il ^a  

^a Kangwon National University   (South Korea)

Author keywords

Bacterial protein glycosylation; Campylobacter jejuni; Crystal structure; N acetyltransferase; PseH

Indexed keywords

ACETIC ACID DERIVATIVE; ACETYL COENZYME A; ACYLTRANSFERASE; BACTERIAL ENZYME; N ACYLTRANSFERASE PSEH; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; CAMPYLOBACTER JEJUNI; CRYSTAL STRUCTURE; ELECTRON; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GLYCOSYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

ACETYL COENZYME A; ACETYLTRANSFERASES; AMINO ACID SEQUENCE; BINDING SITES; CAMPYLOBACTER JEJUNI; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

EID: 84925494581     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.02.041     Document Type: Article

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