PDBsum entry 2aiu

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protein ligands links
Electron transport PDB id
Protein chain
104 a.a. *
PO4 ×2
Waters ×224
* Residue conservation analysis
PDB id:
Name: Electron transport
Title: Crystal structure of mouse testicular cytochromE C at 1.6 angstrom
Structure: CytochromE C, testis-specific. Chain: a. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.60Å     R-factor:   0.178     R-free:   0.207
Authors: Z.Liu,S.Ye,H.Lin,Z.Rao,X.J.Liu
Key ref:
Z.Liu et al. (2006). Remarkably high activities of testicular cytochrome c in destroying reactive oxygen species and in triggering apoptosis. Proc Natl Acad Sci U S A, 103, 8965-8970. PubMed id: 16757556 DOI: 10.1073/pnas.0603327103
01-Aug-05     Release date:   18-Jul-06    
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Protein chain
Pfam   ArchSchema ?
P00015  (CYC2_MOUSE) -  Cytochrome c, testis-specific
105 a.a.
104 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     respiratory chain   3 terms 
  Biological process     positive regulation of intrinsic apoptotic signaling pathway   4 terms 
  Biochemical function     electron carrier activity     4 terms  


DOI no: 10.1073/pnas.0603327103 Proc Natl Acad Sci U S A 103:8965-8970 (2006)
PubMed id: 16757556  
Remarkably high activities of testicular cytochrome c in destroying reactive oxygen species and in triggering apoptosis.
Z.Liu, H.Lin, S.Ye, Q.Y.Liu, Z.Meng, C.M.Zhang, Y.Xia, E.Margoliash, Z.Rao, X.J.Liu.
Hydrogen peroxide (H(2)O(2)) is the major reactive oxygen species (ROS) produced in sperm. High concentrations of H(2)O(2) in sperm induce nuclear DNA fragmentation and lipid peroxidation and result in cell death. The respiratory chain of the mitochondrion is one of the most productive ROS generating systems in sperm, and thus the destruction of ROS in mitochondria is critical for the cell. It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. In our studies, we found that mouse testis-specific cytochrome c (T-Cc) can catalyze the reduction of H(2)O(2) three times faster than its counterpart in somatic cells (S-Cc) and that the T-Cc heme has the greater resistance to being degraded by H(2)O(2). Together, these findings strongly imply that T-Cc can protect sperm from the damages caused by H(2)O(2). Moreover, the apoptotic activity of T-Cc is three to five times greater than that of S-Cc in a well established apoptosis measurement system using Xenopus egg extract. The dramatically stronger apoptotic activity of T-Cc might be important for the suicide of male germ cells, considered a physiological mechanism that regulates the number of sperm produced and eliminates those with damaged DNA. Thus, it is very likely that T-Cc has evolved to guarantee the biological integrity of sperm produced in mammalian testis.
  Selected figure(s)  
Figure 1.
Fig. 1. Schematic diagram of T-Cc illustrated from the proximal side, as viewed from the heme opening of the molecule. Backbones are drawn with the ribbon model and colored white. The 14 residues different to those in S-Cc are shown in the ball and stick model and colored orange. Five water molecules located in the internal part of the protein are in cyan.
Figure 4.
Fig. 4. The region around the Arg-38 site in T-Cc (A) and hh-Cc (B). Water molecules are shown as cyan spheres. Possible hydrogen bond interactions are marked as black dashed lines. The ferric ion in the center of the heme is shown as an orange sphere. The carbon, oxygen, and nitrogen atoms are in yellow, red, and blue, respectively.
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21128733 C.Bischin, F.Deac, R.Silaghi-Dumitrescu, J.A.Worrall, B.S.Rajagopal, G.Damian, and C.E.Cooper (2011).
Ascorbate peroxidase activity of cytochrome c.
  Free Radic Res, 45, 439-444.  
21296189 M.Hüttemann, P.Pecina, M.Rainbolt, T.H.Sanderson, V.E.Kagan, L.Samavati, J.W.Doan, and I.Lee (2011).
The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis.
  Mitochondrion, 11, 369-381.  
20801213 E.Sedlák, M.Fabian, N.C.Robinson, and A.Musatov (2010).
Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage.
  Free Radic Biol Med, 49, 1574-1581.  
20307287 V.P.Shcherbakov (2010).
Biological species is the only possible form of existence for higher organisms: the evolutionary meaning of sexual reproduction.
  Biol Direct, 5, 14.  
19324792 D.K.Dowling, and L.W.Simmons (2009).
Reactive oxygen species as universal constraints in life-history evolution.
  Proc Biol Sci, 276, 1737-1745.  
19414527 J.Ramalho-Santos, S.Varum, S.Amaral, P.C.Mota, A.P.Sousa, and A.Amaral (2009).
Mitochondrial functionality in reproduction: from gonads and gametes to embryos and embryonic stem cells.
  Hum Reprod Update, 15, 553-572.  
19584038 S.G.Fekete, E.Andrásofszky, and R.Glávits (2009).
Pathological changes induced by rancid feed in rats and effects on growth and protein utilisation.
  Acta Vet Hung, 57, 247-261.  
18471988 H.Yu, I.Lee, A.R.Salomon, K.Yu, and M.Hüttemann (2008).
Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration.
  Biochim Biophys Acta, 1777, 1066-1071.  
18843528 M.Hüttemann, I.Lee, A.Pecinova, P.Pecina, K.Przyklenk, and J.W.Doan (2008).
Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease.
  J Bioenerg Biomembr, 40, 445-456.  
  19794904 R.J.Aitken, and S.D.Roman (2008).
Antioxidant systems and oxidative stress in the testes.
  Oxid Med Cell Longev, 1, 15-24.  
18280006 T.Pizzari, R.Dean, A.Pacey, H.Moore, and M.B.Bonsall (2008).
The evolutionary ecology of pre- and post-meiotic sperm senescence.
  Trends Ecol Evol, 23, 131-140.  
18240421 M.Hüttemann, I.Lee, L.Samavati, H.Yu, and J.W.Doan (2007).
Regulation of mitochondrial oxidative phosphorylation through cell signaling.
  Biochim Biophys Acta, 1773, 1701-1720.  
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.