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

Aram Chang, Shanteri Singh, Craig A. Bingman, Jon S. Thorson, George N. Phillips

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

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.

Original languageEnglish
Pages (from-to)197-203
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume67
Issue number3
DOIs
StatePublished - Mar 2011

Keywords

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

ASJC Scopus subject areas

  • Structural Biology

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