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

  • Chang A
  • Singh S
  • Bingman C
 et al. 
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Abstract

The X-ray structure determination at 2.4 A 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.

Author-supplied keywords

  • S-adenosylmethionine
  • acyl carrier proteins
  • biosynthesis
  • enediynes
  • natural products
  • polyketides

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