PDBsum entry 2het

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protein metals Protein-protein interface(s) links
Metal binding protein PDB id
Protein chains
182 a.a. *
_CA ×4
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Non-myristoylated bovine recoverin (truncated at c-terminus) calcium bound to ef-hand 3
Structure: Recoverin. Chain: a, b, c, d. Synonym: p26. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Gene: rcv1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Tetramer (from PQS)
3.00Å     R-factor:   0.237     R-free:   0.259
Authors: O.H.Weiergraber,J.Granzin
Key ref:
O.H.Weiergräber et al. (2006). Tuning of a neuronal calcium sensor. J Biol Chem, 281, 37594-37602. PubMed id: 17015448 DOI: 10.1074/jbc.M603700200
22-Jun-06     Release date:   17-Oct-06    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P21457  (RECO_BOVIN) -  Recoverin
202 a.a.
182 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytosol   1 term 
  Biological process     response to stimulus   4 terms 
  Biochemical function     protein binding     3 terms  


DOI no: 10.1074/jbc.M603700200 J Biol Chem 281:37594-37602 (2006)
PubMed id: 17015448  
Tuning of a neuronal calcium sensor.
O.H.Weiergräber, I.I.Senin, E.Y.Zernii, V.A.Churumova, N.A.Kovaleva, A.A.Nazipova, S.E.Permyakov, E.A.Permyakov, P.P.Philippov, J.Granzin, K.W.Koch.
Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
  Selected figure(s)  
Figure 4.
FIGURE 4. A, tetramer constituting the asymmetric unit of the Rc^2-190 crystals described in this study. Orange spheres represent the Ca^2+ ions bound to EF-hand 3 in each molecule. The position of the 4-fold non-crystallographic axis is indicated. B, segments in the crystal structure of Rc^2-190 (shown in red or orange and numbered I through V) differing significantly from the wild-type (1OMR, gray). The C-terminal tail missing in the truncation mutant is shown in blue. Both views are related by a 45° rotation about the horizontal axis. See text for details.
Figure 6.
FIGURE 6. Stereo representation showing the hydrophobic cluster linking Ile^186 and Phe^188 to apolar residues in EF-hand 3 (green) and EF-hand 4 (yellow). The ribbon backbone is prepared from wild-type coordinates. Side chains of the wild-type protein are indicated in gray, those of the Rc^2-190 mutant in red. The most significant differences are observed for Phe^188 and Trp^104.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 37594-37602) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21118669 V.Parpura, V.Grubišić, and A.Verkhratsky (2011).
Ca(2+) sources for the exocytotic release of glutamate from astrocytes.
  Biochim Biophys Acta, 1813, 984-991.  
20170488 A.Sánchez-Gracia, J.Romero-Pozuelo, and A.Ferrús (2010).
Two frequenins in Drosophila: unveiling the evolutionary history of an unusual neuronal calcium sensor (NCS) duplication.
  BMC Evol Biol, 10, 54.  
18034895 I.I.Senin, V.A.Churumova, P.P.Philippov, and K.W.Koch (2007).
Membrane binding of the neuronal calcium sensor recoverin - modulatory role of the charged carboxy-terminus.
  BMC Biochem, 8, 24.  
17311005 R.D.Burgoyne (2007).
Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling.
  Nat Rev Neurosci, 8, 182-193.  
18074396 R.L.Rich, and D.G.Myszka (2007).
Survey of the year 2006 commercial optical biosensor literature.
  J Mol Recognit, 20, 300-366.  
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.