3LST

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

3LST の概要

• エントリーDOI: 10.2210/pdb3lst/pdb
• 分子名称: CalO1 Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: calicheamicin, methyltransferase, calo1, enediyne, sah, structural genomics, psi-2, protein structure initiative, center for eukaryotic structural genomics, cesg, transferase
• 由来する生物種: Micromonospora echinospora (Micromonospora purpurea)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76765.12

構造登録者

Chang, A.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2010-02-12, 公開日: 2010-03-02, 最終更新日: 2024-10-16)

主引用文献

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

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: 21358050
DOI: 10.1107/S090744491100360X

実験手法

X-RAY DIFFRACTION (2.4 Å)