首页> 美国卫生研究院文献>Acta Crystallographica Section D: Biological Crystallography >Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway
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Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway

机译:CalO1的结构特征:加利车霉素生物合成途径中假定的奥数酸甲基转移酶

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摘要

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.
机译:报道了涉及加利车霉素生物合成的原奥数酸C3 O-甲基转移酶(CalO1)的X射线结构测定为2.4Å。将CalO1与功能相关的加利车霉素奥山梨酸C2 O-甲基转移酶(CalO6)的同源性模型进行比较,可能会涉及多个可能有助于烷基化区域特异性的残基。与提出的对酰基载体蛋白结合的底物的要求相一致,该结构研究还揭示了CalO1中的结构决定簇,这些决定簇有望与酰基载体蛋白结合。

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