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Journal Article
Research Support, Non-U.S. Gov't
Structural analysis of SgvP involved in carbon-sulfur bond formation during griseoviridin biosynthesis.
FEBS Letters 2017 May
Griseoviridin (GV) is a broad-spectrum antibiotic with antibacterial and antifungal activity. In the GV biosynthetic pathway, SgvP catalyzes formation of the carbon-sulfur bond in GV. Herein, we report the recombinant expression and characterization of SgvP from Streptomyces griseoviridis NRRL2427. We also present the 2.6 Å crystal structure of SgvP, which is the first structure of a cytochrome P450 involved in carbon-sulfur bond formation in GV. Structural analysis indicates that Pro237 in the I-helix of SgvP may play a critical role in dioxygen binding and proton transfer during the catalytic cycle. Of the three channels we observed in SgvP, channel 3 may be essential for substrate ingress and egress from the active site, while channels 1 and 2 may be the solvent and water pathway, respectively.
DATABASE: Coordinate and structure factor were deposited in the Protein Data Bank database under the accession number 4MM0.
DATABASE: Coordinate and structure factor were deposited in the Protein Data Bank database under the accession number 4MM0.
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