The three-dimensional structure of carnocyclin A reveals that many circular bacteriocins share a common structural motif

Journal of Biological Chemistry

Volumn 284, Issue 42, 2009, Pages 28674-28681

  Martin Visscher, Leah A ^a   Gong, Xiandi ^a   Duszyk, Marek ^a   Vederas, John C ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE BOND; AMINO ACID PEPTIDES; ANION BINDING; ANTIMICROBIAL PEPTIDE; BACTERIOCINS; BROAD SPECTRUM; DEGRADING ENZYMES; ENTEROCIN; FLUORIDE ION; GRAM-POSITIVE ORGANISMS; HALIDE ANIONS; HYDROPHOBIC CORE; MEMBRANE CHANNELS; NMR STUDIES; OLIGOMERIC STATE; SEQUENCE IDENTITY; SOLUTION STRUCTURES; STRUCTURAL MOTIFS; THREE-DIMENSIONAL STRUCTURE;

AMIDES; AMINO ACIDS; BINDING ENERGY; LIPID BILAYERS; MAMMALS; NEGATIVE IONS; NUCLEAR MAGNETIC RESONANCE; ORGANIC ACIDS; PEPTIDES; THREE DIMENSIONAL;

AMINES;

ANTIBIOTIC AS 48; BACTERIOCIN; CARNOCYCLIN A; HALIDE; UNCLASSIFIED DRUG;

ARTICLE; CARNOBACTERIUM MALTAROMATICUM; CONTROLLED STUDY; DRUG BINDING; DRUG STRUCTURE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIOCINS; ION CHANNELS; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PEPTIDES, CYCLIC; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SAPOSINS; SEQUENCE HOMOLOGY, AMINO ACID;

CARNOBACTERIUM MALTAROMATICUM; MAMMALIA; POSIBACTERIA;

EID: 70350418770     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.036459     Document Type: Article

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