PDBsum entry 1zmz

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protein links
Structural protein PDB id
Protein chain
98 a.a. *
* Residue conservation analysis
PDB id:
Name: Structural protein
Title: Solution structure of the n-terminal domain (m1-s98) of human centrin 2
Structure: Centrin-2. Chain: a. Fragment: n-terminal domain (m1-s98). Synonym: caltractin isoform 1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cetn2, calt, cen2. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: A.Yang,S.Miron,P.Duchambon,L.Assairi,Y.Blouquit,C.T.Craescu
Key ref:
A.Yang et al. (2006). The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly. Biochemistry, 45, 880-889. PubMed id: 16411764 DOI: 10.1021/bi051397s
11-May-05     Release date:   25-Apr-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P41208  (CETN2_HUMAN) -  Centrin-2
172 a.a.
98 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     nucleotide-excision repair   1 term 
  Biochemical function     calcium ion binding     1 term  


DOI no: 10.1021/bi051397s Biochemistry 45:880-889 (2006)
PubMed id: 16411764  
The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly.
A.Yang, S.Miron, P.Duchambon, L.Assairi, Y.Blouquit, C.T.Craescu.
Centrins are well-conserved calcium binding proteins from the EF-hand superfamily implicated in various cellular functions, such as centrosome duplication, DNA repair, and nuclear mRNA export. The intrinsic molecular flexibility and the self-association tendency make difficult the structural characterization of the integral protein. In this paper we report the solution structure, the Ca2+ binding properties, and the intermolecular interactions of the N-terminal domain of two human centrin isoforms, HsCen1 and HsCen2. In the absence of Ca2+, the N-terminal construct of HsCen2 revealed a compact core conformation including four almost antiparallel alpha-helices and a short antiparallel beta-sheet, very similar to the apo state structure of other calcium regulatory EF-hand domains. The first 25 residues show a highly irregular and dynamic structure. The three-dimensional model for the N-terminal domain of HsCen1, based on the high sequence conservation and NMR spectroscopic data, shows very close structural properties. Ca2+ titration of the apo-N-terminal domain of HsCen1 and HsCen2, monitored by NMR spectroscopy, revealed a very weak affinity (10(2)-10(3) M(-1)), suggesting that the cellular role of this domain is not calcium dependent. Isothermal calorimetric titrations showed that an 18-residue peptide, derived from the N-terminal unstructured fragment, has a significant affinity (approximately 10(5) M(-1)) for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21078120 H.Fraga, T.Q.Faria, F.Pinto, A.Almeida, R.M.Brito, and A.M.Damas (2010).
FH8--a small EF-hand protein from Fasciola hepatica.
  FEBS J, 277, 5072-5085.  
20429020 L.Duan, W.Liu, Z.J.Wang, A.H.Liang, and B.S.Yang (2010).
Critical role of tyrosine 79 in the fluorescence resonance energy transfer and terbium(III)-dependent self-assembly of ciliate Euplotes octocarinatus centrin.
  J Biol Inorg Chem, 15, 995.  
18223007 G.Gibrat, F.L.Assairi, Y.Blouquit, C.T.Craescu, and M.C.Bellissent-Funel (2008).
Biophysical study of thermal denaturation of apo-calmodulin: dynamics of native and unfolded states.
  Biophys J, 95, 5247-5256.  
18172010 K.K.Resendes, B.A.Rasala, and D.J.Forbes (2008).
Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export.
  Mol Cell Biol, 28, 1755-1769.  
18200608 O.Okhrimenko, and I.Jelesarov (2008).
A survey of the year 2006 literature on applications of isothermal titration calorimetry.
  J Mol Recognit, 21, 1.  
18329314 P.Trojan, N.Krauss, H.W.Choe, A.Giessl, A.Pulvermüller, and U.Wolfrum (2008).
Centrins in retinal photoreceptor cells: regulators in the connecting cilium.
  Prog Retin Eye Res, 27, 237-259.  
17675401 D.Gogendeau, J.Beisson, Loubresse, J.P.Le Caer, F.Ruiz, J.Cohen, L.Sperling, F.Koll, and C.Klotz (2007).
An Sfi1p-like centrin-binding protein mediates centrin-based Ca2+ -dependent contractility in Paramecium tetraurelia.
  Eukaryot Cell, 6, 1992-2000.  
17603931 Y.Blouquit, P.Duchambon, E.Brun, S.Marco, F.Rusconi, and C.Sicard-Roselli (2007).
High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target.
  Free Radic Biol Med, 43, 216-228.  
  16820684 J.B.Charbonnier, P.Christova, A.Shosheva, E.Stura, M.H.Le Du, Y.Blouquit, P.Duchambon, S.Miron, and C.T.Craescu (2006).
Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 649-651.  
16956364 J.Martinez-Sanz, A.Yang, Y.Blouquit, P.Duchambon, L.Assairi, and C.T.Craescu (2006).
Binding of human centrin 2 to the centrosomal protein hSfi1.
  FEBS J, 273, 4504-4515.  
16627479 J.R.Thompson, Z.C.Ryan, J.L.Salisbury, and R.Kumar (2006).
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.
  J Biol Chem, 281, 18746-18752.
PDB code: 2ggm
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