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Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. doi: 10.1107/S090744491100360X. Epub 2011 Feb 15.

Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.

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1
Department 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.

PMID:
21358050
PMCID:
PMC3046457
DOI:
10.1107/S090744491100360X
[Indexed for MEDLINE]
Free PMC Article
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