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Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound formCrystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.,Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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