PDBsum entry 1m39

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protein links
Cell cycle PDB id
Protein chain
80 a.a. *
* Residue conservation analysis
PDB id:
Name: Cell cycle
Title: Solution structure of thE C-terminal fragment (f86-i165) of the human centrin 2 in calcium saturated form
Structure: Caltractin, isoform 1. Chain: a. Fragment: c-terminus (residues 84-172). Synonym: centrin 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cen2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 25 models
Authors: E.Matei,S.Miron,Y.Blouquit,P.Duchambon,P.Durussel,J.A.Cox, C.T.Craescu
Key ref:
E.Matei et al. (2003). C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain. Biochemistry, 42, 1439-1450. PubMed id: 12578356 DOI: 10.1021/bi0269714
27-Jun-02     Release date:   25-Mar-03    
Go to PROCHECK summary

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

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleic acid binding     4 terms  


DOI no: 10.1021/bi0269714 Biochemistry 42:1439-1450 (2003)
PubMed id: 12578356  
C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain.
E.Matei, S.Miron, Y.Blouquit, P.Duchambon, I.Durussel, J.A.Cox, C.T.Craescu.
Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172), having 10 additional residues. Both fragments are highly disordered in the apo state but become better structured (although not conformationally homogeneous) in the presence of Ca(2+) and depending on the nature of the cations (K(+) or Na(+)) in the buffer. Only the longer C-terminal domain, in the Ca(2+)-saturated state and in the presence of Na(+) ions, was amenable to structure determination by nuclear magnetic resonance. The solution structure of LC-HsCen2 reveals an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. Unexpectedly, the N-terminal helix segment (F86-T94) lies over the exposed hydrophobic cavity. This unusual intramolecular interaction increases considerably the Ca(2+) affinity and constitutes a useful model for the target binding.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
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.  
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.  
16317001 J.H.Sheehan, C.G.Bunick, H.Hu, P.A.Fagan, S.M.Meyn, and W.J.Chazin (2006).
Structure of the N-terminal calcium sensor domain of centrin reveals the biochemical basis for domain-specific function.
  J Biol Chem, 281, 2876-2881.
PDB code: 2ami
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
16786311 L.Liang, S.Flury, V.Kalck, B.Hohn, and J.Molinier (2006).
CENTRIN2 interacts with the Arabidopsis homolog of the human XPC protein (AtRAD4) and contributes to efficient synthesis-dependent repair of bulky DNA lesions.
  Plant Mol Biol, 61, 345-356.  
16750384 T.A.Craig, L.M.Benson, H.R.Bergen, S.Y.Venyaminov, J.L.Salisbury, Z.C.Ryan, J.R.Thompson, J.Sperry, M.L.Gross, and R.Kumar (2006).
Metal-binding properties of human centrin-2 determined by micro-electrospray ionization mass spectrometry and UV spectroscopy.
  J Am Soc Mass Spectrom, 17, 1158-1171.  
  16511082 J.H.Park, N.Krauss, A.Pulvermüller, P.Scheerer, W.Höhne, A.Giessl, U.Wolfrum, K.P.Hofmann, O.P.Ernst, and H.W.Choe (2005).
Crystallization and preliminary X-ray studies of mouse centrin1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 510-513.  
15964821 R.Nishi, Y.Okuda, E.Watanabe, T.Mori, S.Iwai, C.Masutani, K.Sugasawa, and F.Hanaoka (2005).
Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.
  Mol Cell Biol, 25, 5664-5674.  
16002651 S.Geimer, and M.Melkonian (2005).
Centrin scaffold in Chlamydomonas reinhardtii revealed by immunoelectron microscopy.
  Eukaryot Cell, 4, 1253-1263.  
14711432 J.L.Salisbury (2004).
Centrosomes: Sfi1p and centrin unravel a structural riddle.
  Curr Biol, 14, R27-R29.  
15356003 M.Tourbez, C.Firanescu, A.Yang, L.Unipan, P.Duchambon, Y.Blouquit, and C.T.Craescu (2004).
Calcium-dependent self-assembly of human centrin 2.
  J Biol Chem, 279, 47672-47680.  
12890685 A.Popescu, S.Miron, Y.Blouquit, P.Duchambon, P.Christova, and C.T.Craescu (2003).
Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin.
  J Biol Chem, 278, 40252-40261.  
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.