FEBS Letters | |
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 | |
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
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