2AFE

Solution Structure of Asl1650, an Acyl Carrier Protein from Anabaena sp. PCC 7120 with a Variant Phosphopantetheinylation-Site Sequence

Summary for 2AFE

• Entry DOI: 10.2210/pdb2afe/pdb
• Related: 2AFD
• NMR Information: BMRB: 6751
• Descriptor: protein Asl1650 (1 entity in total)
• Functional Keywords: twisted antiparallel helical bundle; acyl carrier protein family, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, ligand binding protein
• Biological source: Nostoc sp.
• Total number of polymer chains: 1
• Total formula weight: 10088.40

Authors

Johnson, M.A.,Peti, W.,Herrmann, T.,Wilson, I.A.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (deposition date: 2005-07-25, release date: 2005-08-16, Last modification date: 2024-05-22)

Primary citation

Johnson, M.A.,Peti, W.,Herrmann, T.,Wilson, I.A.,Wuthrich, K.
Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence
Protein Sci., 15:1030-1041, 2006

PubMed 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.

PubMed: 16597827
DOI: 10.1110/ps.051964606

Experimental method

SOLUTION NMR