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Solution structure of as11650, an acyl carrier protein from anabaena sp pcc 7120 with a variant phosphopantetheinylation-site sequence

Academic Article
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Overview

authors

  • Johnson, M. A.
  • Peti, W.
  • Herrmann, T.
  • Wilson, Ian
  • Wuthrich, Kurt

publication date

  • May 2006

journal

  • Protein Science  Journal

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.

subject areas

  • Acyl Carrier Protein
  • Amino Acid Sequence
  • Anabaena
  • Base Sequence
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Pantetheine
  • Peptide Synthases
  • Polyketide Synthases
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
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Research

keywords

  • NMR structure determination
  • acyl carrier protein
  • cyanobacteria
  • nonribosomal peptide synthetases
  • peptidyl carrier protein
  • polyketide synthases
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Identity

PubMed Central ID

  • PMC2242512

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1110/ps.051964606

PubMed ID

  • 16597827
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Additional Document Info

start page

  • 1030

end page

  • 1041

volume

  • 15

issue

  • 5

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