来自天蓝色链霉菌A3(2)的放线紫红素聚酮合酶酰基载体蛋白与来自大肠杆菌的脂肪酸合酶酰基载体蛋白中的保守二级结构。

Conserved secondary structure in the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2) and the fatty acid synthase acyl carrier protein from Escherichia coli.

作者信息

Crump M P, Crosby J, Dempsey C E, Murray M, Hopwood D A, Simpson T J

机构信息

School of Chemistry, University of Bristol Molecular Recognition Centre, UK.

出版信息

FEBS Lett. 1996 Aug 12;391(3):302-6. doi: 10.1016/0014-5793(96)00756-9.

DOI:10.1016/0014-5793(96)00756-9

PMID:8764994

Abstract

The acyl carrier protein (ACP) of Streptomyces coelicolor A3(2) functions as a molecular chaperone during the biosynthesis of the polyketide actinorhodin (act). Here we compare structural features of the polyketide synthase (PKS) ACP, determined by two-dimensional 1H-NMR, with the Escherichia coli fatty acid synthase (FAS) ACP. The PKS ACP contains four helices (residues 7-16 [A], 42-53 [B], 62-67 [C], 72-86 [D]), and a large loop (residues 17-41) having no defined secondary structure with the exception of a turn between residues 21 and 24. The act ACP shows 47% sequence similarity with the E. coli FAS ACP and the results demonstrate that the sequence homology is extended to the secondary structure of the proteins.

摘要

天蓝色链霉菌A3(2)的酰基载体蛋白（ACP）在聚酮化合物放线紫红素（act）的生物合成过程中作为分子伴侣发挥作用。在此，我们将通过二维1H-NMR测定的聚酮合酶（PKS）ACP的结构特征与大肠杆菌脂肪酸合酶（FAS）ACP进行比较。PKS ACP包含四个螺旋（残基7 - 16 [A]、42 - 53 [B]、62 - 67 [C]、72 - 86 [D]），以及一个除了21和24位残基之间的转角外没有明确二级结构的大环（残基17 - 41）。放线紫红素ACP与大肠杆菌FAS ACP显示出47%的序列相似性，结果表明序列同源性延伸至蛋白质的二级结构。