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PDBsum entry 2k0f
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Metal binding protein
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PDB id
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2k0f
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References listed in PDB file
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Key reference
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Title
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A coupled equilibrium shift mechanism in calmodulin-Mediated signal transduction.
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Authors
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J.Gsponer,
J.Christodoulou,
A.Cavalli,
J.M.Bui,
B.Richter,
C.M.Dobson,
M.Vendruscolo.
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Ref.
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Structure, 2008,
16,
736-746.
[DOI no: ]
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PubMed id
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Abstract
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We used nuclear magnetic resonance data to determine ensembles of conformations
representing the structure and dynamics of calmodulin (CaM) in the calcium-bound
state (Ca(2+)-CaM) and in the state bound to myosin light chain kinase
(CaM-MLCK). These ensembles reveal that the Ca(2+)-CaM state includes a range of
structures similar to those present when CaM is bound to MLCK. Detailed analysis
of the ensembles demonstrates that correlated motions within the Ca(2+)-CaM
state direct the structural fluctuations toward complex-like substates. This
phenomenon enables initial ligation of MLCK at the C-terminal domain of CaM and
induces a population shift among the substates accessible to the N-terminal
domain, thus giving rise to the cooperativity associated with binding. Based on
these results and the combination of modern free energy landscape theory with
classical allostery models, we suggest that a coupled equilibrium shift
mechanism controls the efficient binding of CaM to a wide range of ligands.
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Figure 4.
Figure 4.
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Figure 7.
Figure 7. Comparison between FRET-Derived Distances and the
Corresponding Ones Calculated from the Ca^2+-CaM Ensemble
The distance distribution measured by FRET between a donor
fluorophore and acceptor fluorophore on residues 34 in the NTD
and 110 in the CTD of Ca^2+-CaM is shown in red; the distance
distribution calculated from the Ca^2+-CaM ensemble is shown in
black. See Johnson, 2006.
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The above figures are
reprinted
from an Open Access publication published by Cell Press:
Structure
(2008,
16,
736-746)
copyright 2008.
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