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.
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.
Crump
M P
MP
School of Chemistry, University of Bristol Molecular Recognition Centre, UK.
Crosby
J
J
Dempsey
C E
CE
Murray
M
M
Hopwood
D A
DA
Simpson
T J
TJ
D000213:Acyl Carrier Protein / Q000737:chemistry*; D000217:Acyltransferases / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D004926:Escherichia coli / Q000201:enzymology*; D064429:Fatty Acid Synthases / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D048630:Polyketide Synthases; D017433:Protein Structure, Secondary; D013302:Streptomyces / Q000201:enzymology*
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D048630:Polyketide Synthases; D000217:Acyltransferases; C087193:polyketide beta-ketoacylsynthase; D064429:Fatty Acid Synthases