Solution structure of Asl1650, an acyl carrier protein from  Anabaena  sp. PCC 7120 with a variant phosphopantetheinylation‐site sequence | Zendy

Johnson Margaret A. | Zendy; Peti Wolfgang | Zendy; Herrmann Torsten | Zendy; Wilson Ian A. | Zendy; Wüthrich Kurt | Zendy

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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.

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