1gwi
THE 1.92 A STRUCTURE OF STREPTOMYCES COELICOLOR A3(2) CYP154C1: A NEW MONOOXYGENASE THAT FUNCTIONALIZES MACROLIDE RING SYSTEMS
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OverviewOverview
Evolutionary links between cytochrome P450 monooxygenases, a superfamily, of extraordinarily divergent heme-thiolate proteins catalyzing a wide, array of NADPH/NADH- and O(2)-dependent reactions, are becoming better, understood because of availability of an increasing number of fully, sequenced genomes. Among other reactions, P450s catalyze the site-specific, oxidation of the precursors to macrolide antibiotics in the genus, Streptomyces introducing regiochemical diversity into the macrolide ring, system, thereby significantly increasing antibiotic activity. Developing, effective uses for Streptomyces enzymes in biosynthetic processes and, bioremediation requires identification and engineering of additional, monooxygenases with activities toward a diverse array of small molecules., To ... [(full description)]
About this StructureAbout this Structure
1GWI is a [Single protein] structure of sequence from [Streptomyces coelicolor] with SO4 and HEM as [ligands]. Structure known Active Site: HEB. Full crystallographic information is available from [OCA].
ReferenceReference
The 1.92-A structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems., Podust LM, Kim Y, Arase M, Neely BA, Beck BJ, Bach H, Sherman DH, Lamb DC, Kelly SL, Waterman MR, J Biol Chem. 2003 Apr 4;278(14):12214-21. Epub 2003 Jan 7. PMID:12519772
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