A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB

Journal of Biological Chemistry

Volumn 289, Issue 2, 2014, Pages 735-746

  Lizak, Christian ^a   Gerber, Sabina ^a,c   Zinne, Daria ^a   Michaud, Gaëlle ^b   Schubert, Mario ^a   Chen, Fan ^a   Bucher, Monika ^a   Darbre, Tamis ^b   Zenobi, Renato ^a   Reymond, Jean Louis ^b   Locher, Kaspar P ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF BERN   (Switzerland)

^c GlycoVaxyn AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

N-LINKED GLYCOSYLATION; OLIGOSACCHARYLTRANSFERASE; SEQUENCE MOTIFS; SUBSTRATE BINDING;

BIOCHEMISTRY; BIOLOGY;

CATALYSIS;

ASPARAGINE; CYSTEINE; DISULFIDE; EXTERNAL LOOP EL5; LIPOOLIGOSACCHARIDE; MEMBRANE ENZYME; OLIGOSACCHARYLTRANSFERASE; POLYPEPTIDE; TYROSINE; UNCLASSIFIED DRUG; VALYLLEUCYLTYROSYLGLUTAMINYLLEUCYLLYSYLPHENYLALANYLTYROSYLVALYLPHENYLALANYLLYSINE;

AMINO ACID SEQUENCE; ARTICLE; CAMPYLOBACTER LARI; CATALYSIS; CONTROLLED STUDY; CROSS LINKING; ENZYME GLYCOSYLATION; ENZYME STRUCTURE; GENE; IN VITRO STUDY; PGLB GENE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION;

CAMPYLOBACTER; CYSTEINE-MEDIATED CROSS-LINKING; ENZYME CATALYSIS; ENZYME KINETICS; ENZYME MECHANISMS; GLYCOPROTEIN BIOSYNTHESIS; GLYCOSYLTRANSFERASES; MEMBRANE ENZYMES; OLIGOSACCHARIDE; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPARAGINE; BACTERIAL PROTEINS; BINDING SITES; BIOCATALYSIS; CAMPYLOBACTER LARI; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSYLATION; HEXOSYLTRANSFERASES; LIPOPOLYSACCHARIDES; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TYROSINE;

EID: 84891916781     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.524751     Document Type: Article

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