Proposed Arrangement of Proteins Forming a Bacterial Type II Polyketide Synthase

被引：10

作者：

Castaldo, Gaetano ^{[1
]}

Zucko, Jurica ^{[2
,3
]}

Heidelberger, Sibylle ^{[1
]}

Vujaklija, Dusica ^{[4
]}

Hranueli, Daslav ^{[2
]}

Cullum, John ^{[3
]}

Wattana-Amorn, Pakorn ^{[5
]}

Crump, Matthew P. ^{[5
]}

Crosby, John ^{[5
]}

Long, Paul F. ^{[1
]}

机构：

[1] Univ London, Sch Pharm, London WC1N 1AX, England

[2] Univ Zagreb, Fac Food Technol & Biotechnol, Zagreb 10000, Croatia

[3] Univ Kaiserslautern, Dept Genet, D-67653 Kaiserslautern, Germany

[4] Rudjer Boskovic Inst, Dept Mol Biol, Zagreb 10002, Croatia

[5] Univ Bristol, Sch Chem, Bristol BS8 1TS, Avon, England

来源：

CHEMISTRY & BIOLOGY | 2008年 / 15卷 / 11期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/j.chembiol.2008.09.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aklanonic acid is synthesized by a type 11 polyketide synthase (PKS) composed of eight protein subunits. The network of protein interactions within this complex was investigated using a yeast two-hybrid system, by coaffinity chromatography and by two different computer-aided protein docking simulations. Results suggest that the ketosynthase (KS) alpha and beta subunits interact with each other, and that the KS alpha subunit also probably interacts with a malonyl-CoA: ACP acyltransferase (DpsD), forming a putative minimal synthase. We speculate that DpsD may physically inhibit the priming reaction, allowing the choice of propionate rather than acetate as the starter unit. We also suggest a structural role for the cyclase (DpsY) in maintaining the overall structural integrity of the complex.

引用

页码：1156 / 1165

页数：10

共 71 条

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