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Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation‐site sequence
Author(s) -
Johnson Margaret A.,
Peti Wolfgang,
Herrmann Torsten,
Wilson Ian A.,
Wüthrich Kurt
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051964606
Subject(s) - nonribosomal peptide , anabaena , polyketide , antiparallel (mathematics) , biology , acyl carrier protein , biochemistry , peptide sequence , cyanobacteria , peptide , anabaena variabilis , structural motif , protein structure , gene , biosynthesis , genetics , bacteria , physics , quantum mechanics , magnetic field
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.