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PDBsum entry 2ggm
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protein metals Protein-protein interface(s) links
Cell cycle PDB id
2ggm

 

 

 

 

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Contents
Protein chains
149 a.a. *
17 a.a. *
Metals
_CA ×4
Waters ×217
* Residue conservation analysis
PDB id:
2ggm
Name: Cell cycle
Title: Human centrin 2 xeroderma pigmentosum group c protein complex
Structure: Centrin-2. Chain: a, b. Synonym: caltractin isoform 1. Engineered: yes. DNA-repair protein complementing xp-c cells. Chain: c, d. Fragment: centrin binding region (residues 846-862). Synonym: xeroderma pigmentosum group c complementing protein, p125. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cetn2, calt, cen2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: naturally occurring sequence in humans.
Biol. unit: Tetramer (from PQS)
Resolution:
2.35Å     R-factor:   0.194     R-free:   0.245
Authors: J.R.Thompson
Key ref:
J.R.Thompson et al. (2006). The structure of the human centrin 2-xeroderma pigmentosum group C protein complex. J Biol Chem, 281, 18746-18752. PubMed id: 16627479 DOI: 10.1074/jbc.M513667200
Date:
24-Mar-06     Release date:   25-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P41208  (CETN2_HUMAN) -  Centrin-2 from Homo sapiens
Seq:
Struc: 		172 a.a.
149 a.a.
Protein chains
Pfam   ArchSchema ?
Q01831  (XPC_HUMAN) -  DNA repair protein complementing XP-C cells from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		940 a.a.
17 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1074/jbc.M513667200 J Biol Chem 281:18746-18752 (2006)
PubMed id: 16627479  
 
 
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.
J.R.Thompson, Z.C.Ryan, J.L.Salisbury, R.Kumar.
 
  ABSTRACT  
 
Human centrin-2 plays a key role in centrosome function and stimulates nucleotide excision repair by binding to the xeroderma pigmentosum group C protein. To determine the structure of human centrin-2 and to develop an understanding of molecular interactions between centrin and xeroderma pigmentosum group C protein, we characterized the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide. Our structure shows that the carboxyl-terminal domain of centrin-2 binds this peptide and two calcium atoms, whereas the amino-terminal lobe is in a closed conformation positioned distantly by an ordered alpha-helical linker. A stretch of the amino-terminal domain unique to centrins appears disordered. Two xeroderma pigmentosum group C peptides both bound to centrin-2 also interact to form an alpha-helical coiled-coil. The interface between centrin-2 and each peptide is predominantly nonpolar, and key hydrophobic residues of XPC have been identified that lead us to propose a novel binding motif for centrin.
 
  Selected figure(s)  
 
Figure 1.
FIGURE 1. Structure of human centrin-2 bound to a human XPC-derived peptide. A, sequence of the HsCen-2 recognition site from HsXPC structurally aligned with sequences of skeletal and smooth muscle myosin light chain kinase (skMLCK and smMLCK) and Kar1p from structures with calmodulin and yeast centrin (or caltractin). The XPC peptide structure consists of residues Asn^847-Arg^863, the HsXPC sequence underlined. Essential HsXPC residues interacting to form -helical coiled-coil are indicated in red. Shaded pink are important HsXPC residues interacting with HsCen-2. Positions numbered "1-5-8-14" of key interfacial residues in skeletal muscle myosin light chain kinase and smooth muscle myosin light chain kinase bound to calmodulin are shown for comparison in purple. B, rainbow ribbon trace of the main chains of HsCen-2 with HsXPC and two bound Ca^2+ metals at the C-terminal domain. An ordered helical linker separates N-terminal (blue)(Nterm) and C-terminal (red)(Cterm) domains. The entire XPC peptide is -helix. C, two complexes are found in the asymmetric unit. They interact solely through bound XPC peptides that form an -helical coiled-coil structure. D, the two independent complex structures are nearly equivalent in overall conformation. 		Figure 3.
FIGURE 3. The two domains of HsCen-2 are compared. A cross-eye stereo image is shown of a superposition of the N-terminal HsCen-2 domain (blue) on the C-terminal domain (red). The N-terminal domain exists in a closed conformation. Relative positions of the two bound calcium atoms (dark green) bound to EF-hands III and IV and the XPC peptide (green) with Trp^848, Leu^851, and Leu^855 are drawn. The helices are numbered with regard to past convention and Table 2 herein.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 18746-18752) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21482720 T.J.Dantas, Y.Wang, P.Lalor, P.Dockery, and C.G.Morrison (2011).
Defective nucleotide excision repair with normal centrosome structures and functions in the absence of all vertebrate centrins.
  J Cell Biol, 193, 307-318.  
20980622 C.H.Yang, C.Kasbek, S.Majumder, A.M.Yusof, and H.A.Fisk (2010).
Mps1 phosphorylation sites regulate the function of centrin 2 in centriole assembly.
  Mol Biol Cell, 21, 4361-4372.  
  20586543 E.Brun, Y.Blouquit, P.Duchambon, C.Malosse, J.Chamot-Rooke, and C.Sicard-Roselli (2010).
Oxidative stress induces mainly human centrin 2 polymerisation.
  Int J Radiat Biol, 86, 657-668.  
20941751 N.Tanaka, M.Goto, A.Kawasaki, T.Sasano, K.Eto, R.Nishi, K.Sugasawa, S.Abe, and H.Saitoh (2010).
An EF-hands protein, centrin-1, is an EGTA-sensitive SUMO-interacting protein in mouse testis.
  Cell Biochem Funct, 28, 604-612.  
18343204 D.L.Croteau, Y.Peng, and B.Van Houten (2008).
DNA repair gets physical: mapping an XPA-binding site on ERCC1.
  DNA Repair (Amst), 7, 819-826.  
  18453711 E.Alfaro, L.d.e.l. .V.Sosa, Z.Sanoguet, B.Pastrana-Ríos, and E.R.Schreiter (2008).
Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 402-404.  
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.  
18160718 L.Chen, and K.Madura (2008).
Centrin/Cdc31 is a novel regulator of protein degradation.
  Mol Cell Biol, 28, 1829-1840.  
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.  
17882165 J.H.Min, and N.P.Pavletich (2007).
Recognition of DNA damage by the Rad4 nucleotide excision repair protein.
  Nature, 449, 570-575.
PDB codes: 2qsf 2qsg 2qsh
17694534 J.L.Salisbury (2007).
A mechanistic view on the evolutionary origin for centrin-based control of centriole duplication.
  J Cell Physiol, 213, 420-428.  
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.  
17109756 V.Srsen, and A.Merdes (2006).
The centrosome and cell proliferation.
  Cell Div, 1, 26.  
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 codes are shown on the right.

 

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