Crystal structure of Brucella abortus deoxyxylulose-5- phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis

Journal of Biological Chemistry

Volumn 287, Issue 19, 2012, Pages 15803-15809

  Pérez Gil, Jordi ^a   Calisto, Bárbara M ^b   Behrendt, Christoph ^c   Kurz, Thomas ^c   Fita, Ignacio ^b   Rodríguez Concepción, Manuel ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^c HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE PATHWAYS; ACTIVE SITE; ANIMAL PATHOGENS; ANTIMICROBIAL DRUG; BROAD SPECTRUM ANTIBIOTICS; BRUCELLA; C-TERMINAL DOMAINS; ISOPRENOID BIOSYNTHESIS; ISOPRENOIDS; PROOF OF CONCEPT; REDUCTOISOMERASE; STRUCTURAL RELATIONSHIP; X RAY CRYSTAL STRUCTURES;

BACTERIA; BIOCHEMISTRY; ENZYMES;

LIPIDS;

1 DEOXY D XYLULOSE 5 PHOSPHATASE REDUCTOISOMERASE; 1 DEOXY D XYLULOSE 5 PHOSPHATASE REDUCTOISOMERASE INHIBITOR; BACTERIAL ENZYME; DEOXYXYLULOSE 5 PHOSPHATE REDUCTOISOMERASE LIKE ENZYME; DIMER; ENZYME INHIBITOR; FOSMIDOMYCIN; ISOPRENOID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; BRUCELLA ABORTUS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SYNTHESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING;

ALDOSE-KETOSE ISOMERASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; BIOCATALYSIS; BRUCELLA ABORTUS; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; ENZYME INHIBITORS; FOSFOMYCIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; OXIDOREDUCTASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TERPENES;

ANIMALIA; BACTERIA (MICROORGANISMS); BARTONELLA; BRUCELLA; BRUCELLA MELITENSIS BIOVAR ABORTUS;

EID: 84860852496     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.354811     Document Type: Article

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