Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa

Journal of Biological Chemistry

Volumn 287, Issue 44, 2012, Pages 37395-37405

  Barreteau, Hélène ^a,b   Tiouajni, Mounira ^a,b   Graille, Marc ^a,b   Josseaume, Nathalie ^c,d,e   Bouhss, Ahmed ^a,b   Patin, Delphine ^a,b   Blanot, Didier ^a,b   Fourgeaud, Martine ^c,d,e   Mainardi, Jean Luc ^c,d,e,f   Arthur, Michel ^c,d,e   Van Tilbeurgh, Herman ^a,b   Mengin Lecreulx, Dominique ^a,b,g   Touzé, Thierry ^a,b  

^a UNIVERSITÉ PARIS SACLAY   (France)

^b CNRS   (France)

^c CENTRE DE RECHERCHE DES CORDELIERS   (France)

^d UNIVERSITÉ PARIS DESCARTES   (France)

^e INSERM   (France)

^f HÔPITAL EUROPÉEN GEORGES POMPIDOU   (France)

^g INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANTIBACTERIAL AGENT; BACTERIOCINS; COLICINS; PEPTIDOGLYCANS; PSEUDOMONAS AERUGINOSA; STRUCTURAL CHARACTERIZATION;

BIOCHEMISTRY; BIOLOGY;

BACTERIA;

BACTERIAL PROTEIN; BACTERIOCIN; COLICIN; HYDROLASE; PROTEIN PAEM; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BACTERIUM ISOLATION; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA PURIFICATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GENE AMPLIFICATION; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PURIFICATION; PSEUDOMONAS AERUGINOSA; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; BACTERIOCINS; CATALYTIC DOMAIN; COLICINS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PHOSPHORIC DIESTER HYDROLASES; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

PSEUDOMONAS AERUGINOSA;

EID: 84868224059     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.406439     Document Type: Article

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