3lst | pdb_00003lst

Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form

spinqualitylabelsall models 3lst, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lst is a 2 chain structure with sequence from Micromonospora echinospora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: EDO, MSE, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8KNE5_MICEC 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 PubMed 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-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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