spacer
spacer

PDBsum entry 1zmz

Go to PDB code: 
protein links
Structural protein PDB id
1zmz
Jmol
Contents
Protein chain
98 a.a. *
* Residue conservation analysis
PDB id:
1zmz
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
Date:
11-May-05     Release date:   25-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Gene Ontology (GO) functional annotation 
  GO annot!
  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.
 
  ABSTRACT  
 
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, N.G.de 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
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.