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PDBsum entry 2k0f
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protein metals Protein-protein interface(s) links
Metal binding protein PDB id
2k0f

 

 

 

 

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Contents
Protein chains
142 a.a. *
19 a.a. *
Metals
_CA ×4
* Residue conservation analysis
PDB id:
2k0f
Name: Metal binding protein
Title: Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase
Structure: Calmodulin. Chain: a. Engineered: yes. 19-mer peptide from myosin light chain kinase. Chain: b. Synonym: 19-mer peptide from telokin. 19-mer peptide from kinase- related protein. Engineered: yes
Source: Homo sapiens. Human. Gene: calm1, calm, cam, cam1. Expressed in: escherichia coli. Synthetic: yes. Other_details: sequence occurs naturally in humans
NMR struc: 160 models
Authors: J.Gsponer,J.Christodoulou,A.Cavalli,J.M.Bui,B.Richter,C.M.Dobson, M.Vendruscolo
Key ref:
J.Gsponer et al. (2008). A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure, 16, 736-746. PubMed id: 18462678 DOI: 10.1016/j.str.2008.02.017
Date:
02-Feb-08     Release date:   10-Jun-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens
Seq:
Struc: 		149 a.a.
142 a.a.
Protein chain
Pfam   ArchSchema ?
P11799  (MYLK_CHICK) -  Myosin light chain kinase, smooth muscle from Gallus gallus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1906 a.a.
19 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chain B: E.C.2.7.11.18  - [myosin light-chain] kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[myosin light chain] + ATP = O-phospho-L-seryl-[myosin light chain] + ADP + H+
2. L-threonyl-[myosin light chain] + ATP = O-phospho-L-threonyl-[myosin light chain] + ADP + H+
L-seryl-[myosin light chain]
 + ATP
 = O-phospho-L-seryl-[myosin light chain]
 + ADP
 + H(+)
L-threonyl-[myosin light chain]
 + ATP
 = O-phospho-L-threonyl-[myosin light chain]
 + ADP
 + H(+)
      Cofactor: Ca(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.str.2008.02.017 Structure 16:736-746 (2008)
PubMed id: 18462678  
 
 
A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.
J.Gsponer, J.Christodoulou, A.Cavalli, J.M.Bui, B.Richter, C.M.Dobson, M.Vendruscolo.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. 		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.
 
  The above figures are reprinted from an Open Access publication published by Cell Press: Structure (2008, 16, 736-746) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21207454 C.Leyrat, M.R.Jensen, E.A.Ribeiro, F.C.Gérard, R.W.Ruigrok, M.Blackledge, and M.Jamin (2011).
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
  Protein Sci, 20, 542-556.  
  20939762 M.Figueroa, M.González-Andrade, A.Sosa-Peinado, A.Madariaga-Mazón, F.Del Río-Portilla, M.d.e.l. .C.González, and R.Mata (2011).
Fluorescence, circular dichroism, NMR, and docking studies of the interaction of the alkaloid malbrancheamide with calmodulin.
  J Enzyme Inhib Med Chem, 26, 378-385.  
21109422 S.R.Tzeng, and C.G.Kalodimos (2011).
Protein dynamics and allostery: an NMR view.
  Curr Opin Struct Biol, 21, 62-67.  
20392129 E.S.Price, M.S.DeVore, and C.K.Johnson (2010).
Detecting intramolecular dynamics and multiple Förster resonance energy transfer states by fluorescence correlation spectroscopy.
  J Phys Chem B, 114, 5895-5902.  
21124984 K.G.Neumüller, K.Elsayad, J.M.Reisecker, M.N.Waxham, and K.G.Heinze (2010).
Photounbinding of calmodulin from a family of CaM binding peptides.
  PLoS One, 5, e14050.  
20890288 L.R.Masterson, C.Cheng, T.Yu, M.Tonelli, A.Kornev, S.S.Taylor, and G.Veglia (2010).
Dynamics connect substrate recognition to catalysis in protein kinase A.
  Nat Chem Biol, 6, 821-828.
PDB code: 3o7l
20541943 P.Csermely, R.Palotai, and R.Nussinov (2010).
Induced fit, conformational selection and independent dynamic segments: an extended view of binding events.
  Trends Biochem Sci, 35, 539-546.  
20052284 S.J.Edelstein, M.I.Stefan, and N.Le Novère (2010).
Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.
  PLoS One, 5, e8449.  
19706521 A.Bakan, and I.Bahar (2009).
The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding.
  Proc Natl Acad Sci U S A, 106, 14349-14354.  
  19416527 A.Kurakin (2009).
Scale-free flow of life: on the biology, economics, and physics of the cell.
  Theor Biol Med Model, 6, 6.  
19666496 A.Vallée-Bélisle, F.Ricci, and K.W.Plaxco (2009).
Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors.
  Proc Natl Acad Sci U S A, 106, 13802-13807.  
19841628 D.D.Boehr, R.Nussinov, and P.E.Wright (2009).
The role of dynamic conformational ensembles in biomolecular recognition.
  Nat Chem Biol, 5, 789-796.  
20041208 M.Fromer, and J.M.Shifman (2009).
Tradeoff between stability and multispecificity in the design of promiscuous proteins.
  PLoS Comput Biol, 5, e1000627.  
19359576 R.G.Smock, and L.M.Gierasch (2009).
Sending signals dynamically.
  Science, 324, 198-203.  
19015511 J.Völker, H.H.Klump, and K.J.Breslauer (2008).
DNA energy landscapes via calorimetric detection of microstate ensembles of metastable macrostates and triplet repeat diseases.
  Proc Natl Acad Sci U S A, 105, 18326-18330.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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