PDBsum entry 1c7v

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protein links
Metal binding protein PDB id
Protein chain
68 a.a. *
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Nmr solution structure of the calcium-bound c-terminal domain (w81-s161) of calcium vector protein from amphioxus
Structure: Calcium vector protein. Chain: a. Fragment: c-terminal domain (residues 81-161). Synonym: cavp. Engineered: yes
Source: Branchiostoma lanceolatum. Amphioxus. Organism_taxid: 7740. Tissue: muscle. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: I.Theret,S.Baladi,J.A.Cox,H.Sakamoto,C.T.Craescu
Key ref:
I.Théret et al. (2000). Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement. Biochemistry, 39, 7920-7926. PubMed id: 10891072 DOI: 10.1021/bi000360z
27-Mar-00     Release date:   12-Apr-00    
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Protein chain
Pfam   ArchSchema ?
P04573  (CAVP_BRALA) -  Calcium vector protein
162 a.a.
68 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  


DOI no: 10.1021/bi000360z Biochemistry 39:7920-7926 (2000)
PubMed id: 10891072  
Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement.
I.Théret, S.Baladi, J.A.Cox, H.Sakamoto, C.T.Craescu.
Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state.

Literature references that cite this PDB file's key reference

  PubMed id Reference
16765896 E.Babini, I.Bertini, F.Capozzi, E.Chirivino, and C.Luchinat (2006).
A structural and dynamic characterization of the EF-hand protein CLSP.
  Structure, 14, 1029-1038.
PDB code: 2b1u
14981509 T.L.Wingo, V.N.Shah, M.E.Anderson, T.P.Lybrand, W.J.Chazin, and J.R.Balser (2004).
An EF-hand in the sodium channel couples intracellular calcium to cardiac excitability.
  Nat Struct Mol Biol, 11, 219-225.  
11266596 H.Aitio, T.Laakso, T.Pihlajamaa, M.Torkkeli, I.Kilpeläinen, T.Drakenberg, R.Serimaa, and A.Annila (2001).
Characterization of apo and partially saturated states of calerythrin, an EF-hand protein from S. erythraea: a molten globule when deprived of Ca(2+).
  Protein Sci, 10, 74-82.  
11420441 I.Théret, J.A.Cox, J.Mispelter, and C.T.Craescu (2001).
Backbone dynamics of the regulatory domain of calcium vector protein, studied by (15)N relaxation at four fields, reveals unique mobility characteristics of the intermotif linker.
  Protein Sci, 10, 1393-1402.  
11274468 S.Baladi, P.O.Tsvetkov, T.V.Petrova, T.Takagi, H.Sakamoto, V.M.Lobachov, A.A.Makarov, and J.A.Cox (2001).
Folding units in calcium vector protein of amphioxus: Structural and functional properties of its amino- and carboxy-terminal halves.
  Protein Sci, 10, 771-778.  
  11248946 D.Kraus, S.Khoury, A.Fendyur, S.G.Kachalsky, T.Abu-Hatoum, and R.Rahamimoff (2000).
Intracellular calcium dynamics--sparks of insight.
  J Basic Clin Physiol Pharmacol, 11, 331-365.  
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