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PDBsum entry 2ge0
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References listed in PDB file
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Key reference
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Title
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Conformational switches modulate protein interactions in peptide antibiotic synthetases.
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Authors
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A.Koglin,
M.R.Mofid,
F.Löhr,
B.Schäfer,
V.V.Rogov,
M.M.Blum,
T.Mittag,
M.A.Marahiel,
F.Bernhard,
V.Dötsch.
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Ref.
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Science, 2006,
312,
273-276.
[DOI no: ]
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PubMed id
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Abstract
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Protein dynamics plays an important role in protein function. Many functionally
important motions occur on the microsecond and low millisecond time scale and
can be characterized by nuclear magnetic resonance relaxation experiments. We
describe the different states of a peptidyl carrier protein (PCP) that play a
crucial role in its function as a peptide shuttle in the nonribosomal peptide
synthetases of the tyrocidine A system. Both apo-PCP (without the bound
4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable
conformations. We show that one of the apo conformations and one of the holo
conformations are identical, whereas the two remaining conformations are only
detectable by nuclear magnetic resonance spectroscopy in either the apo or holo
form. We further demonstrate that this conformational diversity is an essential
prerequisite for the directed movement of the 4'-PP cofactor and its interaction
with externally acting proteins such as thioesterases and 4'-PP transferase.
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Figure 1.
Fig. 1. Ribbon diagrams of the average NMR solution structures
of the TycC3-PCP conformers in the A, A/H, and H states.
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Figure 4.
Fig. 4. Model of the A-state TycC3-PCP/Sfp complex. The Sfp
protein is shown in yellow, TycC3-PCP in blue, and CoA in red.
The arrow indicates the position of the reactive thiol group of
CoA. (A) Proposed position of CoA in Sfp based on the electron
density of the adenyl phosphorus in the Sfp crystal structure
(11) and calculations with the program auto-Dock 3 (27). (B)
Space-filling model of the Sfp/A-state TycC3-PCP complex.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2006,
312,
273-276)
copyright 2006.
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Secondary reference #1
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Title
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Crystal structure of the surfactin synthetase-Activating enzyme sfp: a prototype of the 4'-Phosphopantetheinyl transferase superfamily.
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Authors
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K.Reuter,
M.R.Mofid,
M.A.Marahiel,
R.Ficner.
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Ref.
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EMBO J, 1999,
18,
6823-6831.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 Stereo view of the experimental MAD electron density
map covering CoA after solvent flattening contoured at 1.7  .
The ribose is clearly present in a 3'-endo conformation leading
to the axial orientation of the 2'-hydroxyl and the horizontal
orientation of the 3'-phosphate group. Electron density can only
be attributed for the two atoms of the pantetheinyl moiety
nearest to the pyrophosphate.
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Figure 4.
Figure 4 Surface representation of SFP in a similar orientation
to that in Figure 1A. Red represents a negative, and blue a
positive electrostatic surface potential.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by Macmillan Publishers Ltd
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