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PDBsum entry 2afd
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Ligand binding protein
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PDB id
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2afd
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References listed in PDB file
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Key reference
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Title
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Solution structure of asl1650, An acyl carrier protein from anabaena sp. Pcc 7120 with a variant phosphopantetheinylation-Site sequence.
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Authors
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M.A.Johnson,
W.Peti,
T.Herrmann,
I.A.Wilson,
K.Wüthrich.
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Ref.
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Protein Sci, 2006,
15,
1030-1041.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 2.
Wall-eye stereo views of the NMR structure of the protein
Asl1650. (A) Bundle of 20 energy-minimized DYANA conformers.
(Blue) Polypeptide backbone, (gold) hydrophobic side chains of
the protein core. The positions of selected hydrophobic core
residues are identified with the sequence numbers. (B) Ribbon
diagram of the Asl1650 conformer with the lowest RMSD to the
mean coordinates of the bundle of 20 conformers in panel A. The
four helices forming a helix bundle (see text) are labeled
[alpha]I, [alpha]II, 3[10](III), and [alpha]IV at their N
termini. The chain-terminal residues [minus sign]3 and 85 are
indicated.
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Figure 4.
Wall-eye stereo view illustrating structural similarity in
the region of the helix 3[10](III) between Asl1650 (blue) and
TycC3 PCP (green). The backbone is represented by a spline
function through the C^[alpha] positions, and the side chain
heavy atoms are shown as stick diagrams. The orientation is such
that side chains in the front right of the figure are exposed on
the protein surface.
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The above figures are
reprinted
from an Open Access publication published by the Protein Society:
Protein Sci
(2006,
15,
1030-1041)
copyright 2006.
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