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

FEBS Letters

Simpson, Thomas J.¹  Crosby, John¹  Crump, Matthew P.¹  Hopwood, David A.²  Murray, Martin¹  Dempsey, Christopher E.³ 

[1] School of Chemistry (University of Bristol Molecular Recognition Centre), Bristol University, Cantock's Close, Bristol BS8 1TS, UK;John Innes Centre, Norwich NR4 7UH, UK;Department of Biochemistry (University of Bristol Molecular Recognition Centre), Bristol University, University Walk, Bristol BS8 1TD, UK

关键词: Polyketide;    Acyl carrier protein;    Streptomyces;    NMR;    Sequential assignment;    Secondary structure;    Global fold;   

DOI  :  10.1016/0014-5793(96)00756-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown