Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

Journal of Biological Chemistry

Volumn 288, Issue 42, 2013, Pages 30223-30235

  Majorek, Karolina A ^a,b,e,f   Kuhn, Misty L ^c,f   Chruszcz, Maksymilian ^a,d,e,f   Anderson, Wayne F ^c,e,f   Minor, Wladek ^a,e,f  

^a UNIVERSITY OF VIRGINIA   (United States)

^b ADAM MICKIEWICZ UNIVERSITY   (Poland)

^c NORTHWESTERN UNIVERSITY   (United States)

^d UNIVERSITY OF SOUTH CAROLINA   (United States)

^e ARGONNE NATIONAL LABORATORY   (United States)

^f Center for Structural Genomics of Infectious Diseases (CSGID)   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; BIOCHEMICAL CHARACTERIZATION; N-ACETYLTRANSFERASES; PSEUDOMONAS AERUGINOSA; SMALL MOLECULES;

ACETYLATION; AMINO ACIDS; ANTIBIOTICS;

PROTEINS;

7 AMINOCEPHALOSPORANIC ACID; ACETYL COENZYME A; ACYLTRANSFERASE; AMMONIUM 2 (AMINOCARBONYL) BENZOATE; BENZOIC ACID DERIVATIVE; CEFALOTIN; CEFIXIME; CEFMETAZOLE; CEFOTAXIME; CEFOXITIN; CEFUROXIME; CEPHALOSPORIN; COENZYME A; HYBRID PROTEIN; HYMECROMONE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTALLOGRAPHY; EUKARYOTE; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; PRIORITY JOURNAL; PROKARYOTE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ACETYLTRANSFERASE; ANTIBIOTICS; CEPHALOSPORIN; CRYSTAL STRUCTURE; ENZYME INHIBITORS; GCN5-RELATED N-ACETYLTRANSFERASE; GNAT; HIGH THROUGHPUT SCREENING (HTS); LYSINE ACETYLATION; PSEUDOMONAS;

ACETYL COENZYME A; ACETYLTRANSFERASES; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BINDING SITES; CEPHALOSPORINS; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; LYSINE; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS AERUGINOSA;

EID: 84886928360     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.501353     Document Type: Article

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