Open AccessStructural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin‐biosynthetic pathway
Author(s) -
Chang Aram,
Singh Shanteri,
Bingman Craig A.,
Thorson Jon S.,
Phillips George N.
Publication year - 2011
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s090744491100360x
Subject(s) - calicheamicin , biosynthesis , biochemistry , methyltransferase , stereochemistry , chemistry , enzyme , homology modeling , biology , methylation , genetics , dna , antibody
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.