Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.

Chang A; Singh S; Bingman CAThorson JSPhillips GN Jr

首页> 外文期刊>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：结构表征CalO1:假定的苷色酸甲基转移酶calicheamicin-biosynthetic途径。

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摘要

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.

机译：决心为2.4 x射线结构解决假定的苷色酸C3O-methyltransferase (CalO1)参与calicheamicin生物合成报道。比较CalO1相同的模型功能上相关calicheamicin苷色酸C2 O-methyltransferase (CalO6)其中牵扯到的人一些残留,可能会导致烷基化的regiospecificity。提出的要求acyl-carrier-protein-bound基质,这结构研究还揭示了结构在预期的CalO1决定因素容纳一个协会酰基载体蛋白质。

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《Acta crystallographica.Section D. Biological crystallography》 |2011年第3期|197-203|共7页
作者
Chang A; Singh S; Bingman CAThorson JSPhillips GN Jr;
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作者单位

Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, Wisconsin 53706, USA.;

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正文语种英语
中图分类化学;
关键词
Methyltransferases; calicheamicin; X RAY STRUCTUREPathwayAcyl Carrier Protein;

机译：Methyltransferases calicheamicin;X RAYSTRUCTUREPathwayAcyl载体蛋白;

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机译：Characterization of putative Cholesterol Recognition/Interaction amino acid Consensus-Like motif ofCampylobacter jejuni Cytolethal Distending Toxin C

Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.

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