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Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic
Aram Chang1, Shanteri Singh, Craig A Bingman
1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Abstract:
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.
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