The crystal structure of PfFabZ, the unique β-hydroxyacyl-ACP dehydratase involved in fatty acid biosynthesis of Plasmodium falciparum

Protein Science

Volumn 14, Issue 6, 2005, Pages 1570-1580

  Kostrewa, Dirk ^a   Winkler, Fritz K ^a   Folkers, Gerd ^b   Scapozza, Leonardo ^c   Perozzo, Remo ^c  

^a PAUL SCHERRER INSTITUTE   (Switzerland)

^b Swiss Federal Institute of Technology Collegium Helveticum   (Switzerland)

^c UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

hydroxyacyl ACP dehydratase; 3 decynoyl N acetylcysteamine; Crystal structure; Drug target; Fatty acid biosynthesis; Malaria; Plasmodium falciparum; SAD phasing

Indexed keywords

3 DECYNOYL N ACETYLCYSTEAMINE; ACETIC ACID DERIVATIVE; BETA HYDROXYACYL ACYL CARRIER PROTEIN DEHYDRATASE; FATTY ACID; HYDROLYASE; POTASSIUM IODIDE; PROTEIN PFFABZ; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG MECHANISM; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; FATTY ACID SYNTHESIS; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; ENOYL-COA HYDRATASE; FATTY ACIDS; MOLECULAR SEQUENCE DATA; PLASMODIUM FALCIPARUM; PROTEIN STRUCTURE, QUATERNARY; PROTOZOAN PROTEINS; SUBSTRATE SPECIFICITY;

CANIS FAMILIARIS; PLASMODIUM FALCIPARUM;

EID: 22544476228     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051373005     Document Type: Article

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