CalO1的结构表征：一种在刺孢霉素生物合成途径中假定的苔色酸甲基转移酶。
Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.
作者信息
Chang Aram, Singh Shanteri, Bingman Craig A, Thorson Jon S, Phillips George N
机构信息
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. doi: 10.1107/S090744491100360X. Epub 2011 Feb 15.
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.
摘要
报道了参与刺孢霉素生物合成的假定苔色酸C3 O-甲基转移酶（CalO1）在2.4 Å分辨率下的X射线结构测定。将CalO1与功能相关的刺孢霉素苔色酸C2 O-甲基转移酶（CalO6）的同源模型进行比较，发现了几个可能有助于烷基化区域特异性的残基。与酰基载体蛋白结合底物的拟议要求一致，这项结构研究还揭示了CalO1内的结构决定因素，预计这些因素可适应与酰基载体蛋白的结合。
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