PDBsum entry 1omv

Go to PDB code: 
protein metals links
Metal binding protein PDB id
Protein chain
188 a.a. *
Waters ×76
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Non-myristoylated bovine recoverin (e85q mutant) with calciu ef-hand 3
Structure: Recoverin. Chain: a. Engineered: yes. Mutation: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Gene: rcv1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
1.90Å     R-factor:   0.240     R-free:   0.249
Authors: O.H.Weiergraber,J.Granzin
Key ref:
O.H.Weiergräber et al. (2003). Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin. J Biol Chem, 278, 22972-22979. PubMed id: 12686556 DOI: 10.1074/jbc.M300447200
26-Feb-03     Release date:   25-Nov-03    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P21457  (RECO_BOVIN) -  Recoverin
202 a.a.
188 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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.M300447200 J Biol Chem 278:22972-22979 (2003)
PubMed id: 12686556  
Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin.
O.H.Weiergräber, I.I.Senin, P.P.Philippov, J.Granzin, K.W.Koch.
Recoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.
  Selected figure(s)  
Figure 7.
FIG. 7. Arrangement of side chains critical for interaction with rhodopsin kinase (as defined in Ref. 41). Residues probably involved in the binding interface according to these authors are colored in red, those of minor significance in orange. Abbreviations are as in Fig. 6.
Figure 8.
FIG. 8. C[ ]trace superposition (identical to Fig. 5 with 180° rotation) of non-myristoylated recoverin with one Ca^2+ (darker colors) and myristoylated recoverin with two Ca^2+ (lighter colors) showing positional re-arrangement of hydrophobic residues forming the patch defined in Fig. 6 (yellow backbone) and of side chains probably (light and dark red) and possibly (light and dark orange) involved in rhodopsin kinase inhibition (see Fig. 7).
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 22972-22979) copyright 2003.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21327964 S.Theisgen, L.Thomas, T.Schröder, C.Lange, M.Kovermann, J.Balbach, and D.Huster (2011).
The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2.
  Eur Biophys J, 40, 565-576.  
18942727 J.L.Li, C.Y.Geng, Y.Bu, X.R.Huang, and C.C.Sun (2009).
Conformational transition pathway in the allosteric process of calcium-induced recoverin: molecular dynamics simulations.
  J Comput Chem, 30, 1135-1145.  
19457073 K.E.Komolov, I.I.Senin, N.A.Kovaleva, M.P.Christoph, V.A.Churumova, I.I.Grigoriev, M.Akhtar, P.P.Philippov, and K.W.Koch (2009).
Mechanism of rhodopsin kinase regulation by recoverin.
  J Neurochem, 110, 72-79.  
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.  
17078090 T.Gensch, K.E.Komolov, I.I.Senin, P.P.Philippov, and K.W.Koch (2007).
Ca2+-dependent conformational changes in the neuronal Ca2+-sensor recoverin probed by the fluorescent dye Alexa647.
  Proteins, 66, 492-499.  
16733800 E.Fik-Rymarkiewicz, T.Duda, and R.K.Sharma (2006).
Novel frequenin-modulated Ca2+-signaling membrane guanylate cyclase (ROS-GC) transduction pathway in bovine hippocampus.
  Mol Cell Biochem, 291, 187-204.  
15843174 K.E.Komolov, D.V.Zinchenko, V.A.Churumova, S.A.Vaganova, O.H.Weiergräber, I.I.Senin, P.P.Philippov, and K.W.Koch (2005).
One of the Ca2+ binding sites of recoverin exclusively controls interaction with rhodopsin kinase.
  Biol Chem, 386, 285-289.  
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.