Crystallization and preliminary X-ray diffraction studies of aclacinomycin-10-methyl esterase and aclacinomycin-10-hydroxylase from Streptomyces purpurascens



: Jansson A, Niemi J, Mantsala P, Schneider G

Publisher: BLACKWELL MUNKSGAARD

: 2003

 Acta Crystallographica Section D: Biological Crystallography

: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

: ACTA CRYSTALLOGR D

: 59

: 1637

: 1639

: 3

: 0907-4449

DOI: https://doi.org/10.1107/S0907444903014100


Two enzymes participating in the biosynthesis of anthracyclines in Streptomyces purpurascens, aclacinomycin-10-methyl esterase (RdmC) and aclacinomycin-10-hydroxylase (RdmB), have been crystallized. RdmB is a S-adenosyl-methionine-dependent hydroxylase and RdmC hydrolyses the carboxymethyl group of the aglycone skeleton of aclacinomycin. Crystals of RdmB obtained in the presence of S-adenosyl-L-methionine were orthorhombic, space group C222(1), with unit-cell parameters a = 63.2, b = 92.2, c = 115.3 Angstrom; diffraction data were collected to 2.1 Angstrom resolution. RdmC was crystallized as a complex with the substrate, aclacinomycin T. These crystals diffracted to 1.45 Angstrom resolution and belonged to space group P2(1), with unit-cell parameters a = 38.2, b = 84.7, c = 44.3 Angstrom, beta = 99.9degrees.



Last updated on 14/10/2025 09:41:10 AM