3LST
Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form
Summary for 3LST
| Entry DOI | 10.2210/pdb3lst/pdb |
| Descriptor | CalO1 Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | calicheamicin, methyltransferase, calo1, enediyne, sah, structural genomics, psi-2, protein structure initiative, center for eukaryotic structural genomics, cesg, transferase |
| Biological source | Micromonospora echinospora (Micromonospora purpurea) |
| Total number of polymer chains | 2 |
| Total formula weight | 76765.12 |
| Authors | Chang, A.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2010-02-12, release date: 2010-03-02, Last modification date: 2024-10-16) |
| Primary citation | Chang, A.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips, G.N. Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway. Acta Crystallogr.,Sect.D, 67:197-203, 2011 Cited by PubMed Abstract: 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. PubMed: 21358050DOI: 10.1107/S090744491100360X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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