The X-ray structure determination at 2.4 Å resolution of the putative orsellinic acid C3 O-methyltransferase (CalO1) involved in calicheamicin biosynthesis is reported. Comparison of CalO1 with a homology model of the functionally related calicheamicin orsellinic acid C2 O-methyltransferase (CalO6) implicates several residues that are likely to contribute to the regiospecificity of alkylation. Consistent with the proposed requirement of an acyl-carrier-protein-bound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein. © 2011 International Union of Crystallography. Printed in Singapore - all rights reserved.
CITATION STYLE
Chang, A., Singh, S., Bingman, C. A., Thorson, J. S., & Phillips, G. N. (2011). Structural characterization of CalO1: A putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway. Acta Crystallographica Section D: Biological Crystallography, 67(3), 197–203. https://doi.org/10.1107/S090744491100360X
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