Crystal structure of aclacinomycin-10-hydroxylase, a S-adenosyl-L- methionine-dependent methyltransferase homolog involved in anthracycline biosynthesis in Streptomyces purpurascens

Journal of Molecular Biology

Volumn 334, Issue 2, 2003, Pages 269-280

  Jansson, Anna ^a   Niemi, Jarmo ^b   Lindqvist, Ylva ^a   Mäntsälä, Pekka ^b   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b UNIVERSITY OF TURKU   (Finland)

Author keywords

Enzyme mechanism; Helix swapping; Protein crystallography; Protein structure; Rhodomycin biosynthesis

Indexed keywords

15 DEMETHOXY EPSILON RHODOMYCIN; ACLACINOMYCIN 10 HYDROXYLASE; ANTHRACYCLINE; ANTIBIOTIC AGENT; BETA RHODOMYCIN; CARUBICIN; CHALCONE; ENZYME; ISOFLAVONE; METHYL GROUP; METHYLTRANSFERASE; NUCLEOTIDE BINDING PROTEIN; PROTEIN; PROTON; S ADENOSYLMETHIONINE; S ADENOSYLMETHIONINE DEPENDENT METHYLTRANSFERASE; TETRACINOMYCIN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BIOSYNTHESIS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; DIFFRACTION; DIMERIZATION; DRUG SYNTHESIS; ENZYME BINDING; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN TRANSPORT; SEQUENCE HOMOLOGY; STREPTOMYCES;

STREPTOMYCES; STREPTOMYCES PURPURASCENS;

EID: 0242383971     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.061     Document Type: Article

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