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

Journal Article · Mon Nov 07 00:00:00 EST 2011 · Acta Crystallogr. D

DOI:https://doi.org/10.1107/S090744491100360X· OSTI ID:1022276

Chang, Aram; Singh, Shanteri; Bingman, Craig A; Thorson, Jon S

The X-ray structure determination at 2.4 {angstrom} 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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: National Institutes of Health (NIH)
• OSTI ID: 1022276
• Journal Information: Acta Crystallogr. D, Vol. 67, Issue (3) ; 03, 2011; ISSN 0907-4449
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
ALKYLATION
BIOSYNTHESIS
PROTEINS
RESIDUES
RESOLUTION