Structure of antibacterial peptide microcin J25: A 21-residue lariat protoknot

Journal of the American Chemical Society

Volumn 125, Issue 41, 2003, Pages 12382-12383

  Bayro, Marvin J ^a   Mukhopadhyay, Jayanta ^a   Swapna, G V T ^a   Huang, Janet Y ^a   Ma, Li Chung ^a   Sineva, Elena ^a   Dawson, Philip E ^b   Montelione, Gaetano T ^a   Ebright, Richard H ^a  

^a RUTGERS UNIVERSITY   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; CARBOXYPEPTIDASE; CYSTEINE; GLUTAMIC ACID; GLYCINE; MICROCIN J25; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT; RNA POLYMERASE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CHEMICAL BOND; CHEMICAL INTERACTION; COVALENT BOND; DRUG MECHANISM; DRUG PROTEIN BINDING; DRUG STRUCTURE; DRUG SYNTHESIS; ESCHERICHIA COLI; GROWTH INHIBITION; ISOMER; MOLECULAR STABILITY; MOLECULAR WEIGHT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; STEREOCHEMISTRY; STRUCTURE ANALYSIS; TRANSCRIPTION REGULATION;

ANTI-BACTERIAL AGENTS; BACTERIOCINS; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 0141988966     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja036677e     Document Type: Article

References (23)

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9. C18, 5 μm, 300 Å column (Rainin; Inc.); solvent A = 0.1% TFA, solvent B = 90% acetonitrile and 0.1% TFA; gradient = 30-35% solvent B in solvent A over a period of 20 min, flow rate = 1 mL/min.
10. gene is the codon number in the gene for MccJ25 precursor.
11. 3OH. Triple-resonance NMR data were collected at 25 °C as described using a Varian INOVA 500 NMR spectrometer. Resonance assignments were determined for all assignable atoms by manual analysis of triple-resonance NMR spectra and have been deposited in the BioMagResDataBase (accession 5859).
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17. 4 exhibits sequence similiarity to amidotransferases of the Asn-synthase/Gln-hydrolase class, which catalyze transfer of ammonia or an amine from an amide donor to a carboxyl acceptor (Ebright, R. H., unpublished results). Processing of MccJ25 involves two reactions: removal of the 37-residue N-terminal pro-sequence (residues -37 to -1) and cyclization of residues 1-8. We suggest that McjC carries out both reactions, acting on pre-folded MccJ25 precursor to catalyze transfer of the α-amino of residue 1 from the backbone amide of residue -1 to the side-chain carboxyl of residue 8.
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