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

Matthew P Crump, J Crosby, CE Dempsey, M Murray, DA Hopwood, TJ Simpson

Research output: Contribution to journalArticle (Academic Journal)peer-review

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 H-1-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.
Translated title of the contributionConserved 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
Original languageEnglish
Pages (from-to)302-306
Number of pages5
JournalFEBS Letters
Volume391
Issue number3
Publication statusPublished - 12 Aug 1996

Bibliographical note

Other: Crump, MP was a Bristol postgraduate, PhD 19/12/95

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