Journal
PROTEIN SCIENCE
Volume 15, Issue 5, Pages 1030-1041Publisher
WILEY
DOI: 10.1110/ps.051964606
Keywords
NMR structure determination; acyl carrier protein; peptidyl carrier protein; polyketide synthases; nonribosomal peptide synthetases; cyanobacteria
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Funding
- NIGMS NIH HHS [P50 GM62411, P50 GM062411] Funding Source: Medline
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Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To gain new insight into the physiological role of acyl carriers in Anabaena, the solution structure of Asl1650 has been solved by NMR spectroscopy. The protein adopts a twisted antiparallel four-helix bundle fold, with a variant phosphopantetheine-attachment motif positioned at the start of the second helix. Structure comparisons with proteins from other organisms suggest a likely physiological function as a discrete peptidyl carrier protein.
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