Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway
✍ Scribed by Chang, Aram ;Singh, Shanteri ;Bingman, Craig A. ;Thorson, Jon S. ;Phillips, George N.
- Publisher
- International Union of Crystallography
- Year
- 2011
- Tongue
- English
- Weight
- 737 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0907-4449
No coin nor oath required. For personal study only.
✦ Synopsis
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-proteinbound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein.