The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule

Journal of Molecular Biology

Volumn 275, Issue 5, 1998, Pages 847-859

  Engel, Christian K ^a   Kiema, Tiila R ^b   Kalervo Hiltunen, J ^b   Wierenga, Rik K ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b UNIVERSITY OF OULU   (Finland)

Author keywords

CoA; Hydratase; Ligand binding; Structure; oxidation

Indexed keywords

ACYL COENZYME A; ENOYL COENZYME A HYDRATASE; GLUTAMIC ACID; LONG CHAIN FATTY ACID;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBUNIT; HYDRATION; HYDROXYLATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING;

EID: 0032488815     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1491     Document Type: Article

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