ArticleProtein science : a publication of the Protein Society2006
Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 17 citations in OpenAlex.
- The Effect of Divalent Cations on the Thermostability of Type II Polyketide Synthase Acyl Carrier Proteins.AIChE journal. American Institute of Chemical Engineers · 2018Article
- Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.The Journal of biological chemistry · 2017Article
- Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.Protein science : a publication of the Protein Society · 2017Article
- Secondary metabolite gene expression and interplay of bacterial functions in a tropical freshwater cyanobacterial bloom.The ISME journal · 2014Article
- Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structure and mechanism of the trans-acting acyltransferase from the disorazole synthase.Biochemistry · 2011Article
- Structural insights into nonribosomal peptide enzymatic assembly lines.Natural product reports · 2009Review
- Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.Nature · 2008Article
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Abstract
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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