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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
Author(s) -
Crump Matthew P.,
Crosby John,
Dempsey Christopher E.,
Murray Martin,
Hopwood David A.,
Simpson Thomas J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00756-9
Subject(s) - actinorhodin , acyl carrier protein , streptomyces coelicolor , polyketide synthase , fatty acid synthase , polyketide , escherichia coli , biochemistry , atp synthase , biology , peptide sequence , streptomyces , stereochemistry , biosynthesis , fatty acid , chemistry , bacteria , enzyme , gene , mutant , genetics
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 1 H‐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.