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Published online before print April 5, 2006, 10.1110/ps.051964606
Protein Science (2006), 15:1030-1041. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence

Margaret A. Johnson, Wolfgang Peti2, Torsten Herrmann2, Ian A. Wilson and Kurt Wüthrich

The Scripps Research Institute (TSRI), Department of Molecular Biology and Joint Center for Structural Genomics (JCSG), La Jolla, California 92037, USA

(RECEIVED November 9, 2005; FINAL REVISION January 26, 2006; ACCEPTED January 28, 2006)

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.

Keywords: NMR structure determination; acyl carrier protein; peptidyl carrier protein; polyketide synthases; nonribosomal peptide synthetases; cyanobacteria


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