spacer
spacer

PDBsum entry 1vrk
Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Complex(calcium-binding protein/peptide) PDB id
1vrk

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
148 a.a. *
21 a.a. *
Ligands
ACT
Metals
_CA ×4
Waters ×141
* Residue conservation analysis
PDB id:
1vrk
Name: Complex(calcium-binding protein/peptide)
Title: The 1.9 angstrom structure of e84k-calmodulin rs20 peptide complex
Structure: Calmodulin. Chain: a. Engineered: yes. Mutation: yes. Rs20. Chain: b. Engineered: yes. Other_details: trp 4 is ne-formylated
Source: Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: consensus sequence from a number of sources.
Biol. unit: Monomer (from PDB file)
Resolution:
1.90Å     R-factor:   0.171     R-free:   0.242
Authors: S.Weigand,W.F.Anderson
Key ref:
S.Mirzoeva et al. (1999). Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties. Biochemistry, 38, 3936-3947. PubMed id: 10194305 DOI: 10.1021/bi9821263
Date:
24-Sep-97     Release date:   27-Apr-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 148 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.
21 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 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: 10.1021/bi9821263 Biochemistry 38:3936-3947 (1999)
PubMed id: 10194305  
 
 
Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties.
S.Mirzoeva, S.Weigand, T.J.Lukas, L.Shuvalova, W.F.Anderson, D.M.Watterson.
 
  ABSTRACT  
 
The enhancement of calmodulin's (CaM) calcium binding activity by an enzyme or a recognition site peptide and its diminution by key point mutations at the protein recognition interface (e.g., E84K-CaM), which is more than 20 A away from the nearest calcium ligation structure, can be described by an expanded version of the Adair-Klotz equation for multiligand binding. The expanded equation can accurately describe the calcium binding events and their variable linkage to protein recognition events can be extended to other CaM-regulated enzymes and can potentially be applied to a diverse array of ligand binding systems with allosteric regulation of ligand binding, whether by other ligands or protein interaction. The 1.9 A resolution X-ray crystallographic structure of the complex between E84K-CaM and RS20 peptide, the CaM recognition site peptide from vertebrate smooth muscle and nonmuscle forms of myosin light chain kinase, provides insight into the structural basis of the functional communication between CaM's calcium ligation structures and protein recognition surfaces. The structure reveals that the complex adapts to the effect of the functional mutation by discrete adjustments in the helix that contains E84. This helix is on the amino-terminal side of the helix-loop-helix structural motif that is the first to be occupied in CaM's calcium binding mechanism. The results reported here are consistent with a sequential and cooperative model of CaM's calcium binding activity in which the two globular and flexible central helix domains are functionally linked, and provide insight into how CaM's calcium binding activity and peptide recognition properties are functionally coupled.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20010694 F.Rodríguez-Castañeda, M.Maestre-Martínez, N.Coudevylle, K.Dimova, H.Junge, N.Lipstein, D.Lee, S.Becker, N.Brose, O.Jahn, T.Carlomagno, and C.Griesinger (2010).
Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity.
  EMBO J, 29, 680-691.
PDB code: 2kdu
19996092 N.Juranic, E.Atanasova, A.G.Filoteo, S.Macura, F.G.Prendergast, J.T.Penniston, and E.E.Strehler (2010).
Calmodulin wraps around its binding domain in the plasma membrane Ca2+ pump anchored by a novel 18-1 motif.
  J Biol Chem, 285, 4015-4024.
PDB code: 2kne
18669651 M.I.Stefan, S.J.Edelstein, and N.Le Novère (2008).
An allosteric model of calmodulin explains differential activation of PP2B and CaMKII.
  Proc Natl Acad Sci U S A, 105, 10768-10773.  
18175310 R.A.Newman, W.S.Van Scyoc, B.R.Sorensen, O.R.Jaren, and M.A.Shea (2008).
Interdomain cooperativity of calmodulin bound to melittin preferentially increases calcium affinity of sites I and II.
  Proteins, 71, 1792-1812.  
17868328 A.Helten, W.Säftel, and K.W.Koch (2007).
Expression level and activity profile of membrane bound guanylate cyclase type 2 in rod outer segments.
  J Neurochem, 103, 1439-1446.  
16877516 J.H.Streiff, T.W.Allen, E.Atanasova, N.Juranic, S.Macura, A.R.Penheiter, and K.A.Jones (2006).
Prediction of volatile anesthetic binding sites in proteins.
  Biophys J, 91, 3405-3414.  
16721661 K.Chen, J.Ruan, and L.A.Kurgan (2006).
Prediction of three dimensional structure of calmodulin.
  Protein J, 25, 57-70.  
16171378 T.I.Igumenova, A.L.Lee, and A.J.Wand (2005).
Backbone and side chain dynamics of mutant calmodulin-peptide complexes.
  Biochemistry, 44, 12627-12639.  
15345523 T.J.Lukas (2004).
A signal transduction pathway model prototype I: From agonist to cellular endpoint.
  Biophys J, 87, 1406-1416.  
12829504 M.Nousiainen, P.J.Derrick, D.Lafitte, and P.Vainiotalo (2003).
Relative affinity constants by electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry: calmodulin binding to peptide analogs of myosin light chain kinase.
  Biophys J, 85, 491-500.  
12542690 S.W.Vetter, and E.Leclerc (2003).
Novel aspects of calmodulin target recognition and activation.
  Eur J Biochem, 270, 404-414.  
12191613 A.V.Velentza, A.M.Schumacher, and D.M.Watterson (2002).
Structure, activity, regulation, and inhibitor discovery for a protein kinase associated with apoptosis and neuronal death.
  Pharmacol Ther, 93, 217-224.  
12414710 H.H.Gan, R.A.Perlow, S.Roy, J.Ko, M.Wu, J.Huang, S.Yan, A.Nicoletta, J.Vafai, D.Sun, L.Wang, J.E.Noah, S.Pasquali, and T.Schlick (2002).
Analysis of protein sequence/structure similarity relationships.
  Biophys J, 83, 2781-2791.  
11266605 G.Larsson, J.Schleucher, J.Onions, S.Hermann, T.Grundström, and S.S.Wijmenga (2001).
A novel target recognition revealed by calmodulin in complex with the basic helix--loop--helix transcription factor SEF2-1/E2-2.
  Protein Sci, 10, 169-186.  
11341924 M.V.Medvedeva, D.R.Djemuchadze, D.M.Watterson, S.B.Marston, and N.B.Gusev (2001).
Replacement of Lys-75 of calmodulin affects its interaction with smooth muscle caldesmon.
  Biochim Biophys Acta, 1544, 143-150.  
10841769 O.R.Jaren, S.Harmon, A.F.Chen, and M.A.Shea (2000).
Paramecium calmodulin mutants defective in ion channel regulation can bind calcium and undergo calcium-induced conformational switching.
  Biochemistry, 39, 6881-6890.  
10852728 T.J.Hill, D.Lafitte, J.I.Wallace, H.J.Cooper, P.O.Tsvetkov, and P.J.Derrick (2000).
Calmodulin-peptide interactions: apocalmodulin binding to the myosin light chain kinase target-site.
  Biochemistry, 39, 7284-7290.  
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.

 

spacer
spacer