PDBsum entry 1om2

Go to PDB code: 
protein Protein-protein interface(s) links
Receptor/oxidoreductase complex PDB id
Protein chains
95 a.a. *
11 a.a. *
* Residue conservation analysis
PDB id:
Name: Receptor/oxidoreductase complex
Title: Solution nmr structure of the mitochondrial protein import receptor tom20 from rat in a complex with a presequence peptide derived from rat aldehyde dehydrogenase (aldh)
Structure: Protein (mitochondrial import receptor subunit tom20). Chain: a. Fragment: residues 51-145. Engineered: yes. Other_details: cytosolic domain, limited proteolyzed fragment. Protein (mitochondrial aldehyde dehydrogenase). Chain: b.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organelle: mitochondria. Cellular_location: mitochondrial outer membrane. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. The
NMR struc: 20 models
Authors: Y.Abe,T.Shodai,T.Muto,K.Mihara,H.Torii,S.Nishikawa,T.Endo, D.Kohda
Key ref:
Y.Abe et al. (2000). Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell, 100, 551-560. PubMed id: 10721992 DOI: 10.1016/S0092-8674(00)80691-1
23-Apr-99     Release date:   02-Feb-00    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q62760  (TOM20_RAT) -  Mitochondrial import receptor subunit TOM20 homolog
145 a.a.
95 a.a.*
Protein chain
Pfam   ArchSchema ?
P11884  (ALDH2_RAT) -  Aldehyde dehydrogenase, mitochondrial
519 a.a.
11 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.  - Aldehyde dehydrogenase (NAD(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An aldehyde + NAD+ + H2O = a carboxylate + NADH
+ NAD(+)
+ H(2)O
= carboxylate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mitochondrial outer membrane translocase complex   1 term 
  Biological process     intracellular protein transport   2 terms 


DOI no: 10.1016/S0092-8674(00)80691-1 Cell 100:551-560 (2000)
PubMed id: 10721992  
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.
Y.Abe, T.Shodai, T.Muto, K.Mihara, H.Torii, S.Nishikawa, T.Endo, D.Kohda.
Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all alpha-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.
  Selected figure(s)  
Figure 3.
Figure 3. Structure of Δ50Tom20 in Complex with a Presequence Peptide, pALDH(12–22)(A) Sequence alignment of Δ50Tom20 and corresponding regions of Tom20 from other organisms (human, Caenorhabditis elegans, Neurospora crassa, and yeast Saccharomyces cerevisiae). The two acidic regions and the Q-rich region are shaded in red and yellow, respectively. The TPR motif is shown as a blue box with its consensus amino acids. α helices and flexible regions are drawn as cylinders and broken lines, respectively. The hydrophobic residues constituting the hydrophobic patch in the presequence binding groove are indicated with yellow triangles, and the hydrophilic residues in the periphery of the groove are colored in orange (Gln) and red (Glu) circles.(B) Overlay of the 20 final structures. The residues used for superimposing the different structures are colored in blue (Tom20) and red (presequence peptide), and the other residues are in gray (Tom20) and orange (presequence).(C) Ribbon model of Δ50Tom20 indicating the {^1H}-^15N heteronuclear NOE values (red to white; −0.9 vert, similar +0.9) measured in the absence of the presequence. Smaller NOE values imply faster motions.
Figure 5.
Figure 5. Representation of the Binding Groove of Δ50Tom20 and the Bound Presequence Peptide(A) Molecular surface of Δ50Tom20 (residues 57–124). Hydrophobic residues comprising the hydrophobic patch (Phe^70, Leu^71, Ile^74, Leu^106, Val^109, Leu^110, Thr^113), and Gln (Gln^67, Gln^75, Gln^102, Gln^104, Gln^105, Gln^108, Gln^111, and Gln^112) and Glu (Glu^78 and Glu^79) in the peripheral region are colored in yellow, orange, and red, respectively. The bound peptide is drawn as a tube with sidechains in magenta for Leu, blue for Arg, and cyan for others. N' and C' denote the N and C termini of the peptide, respectively.(B) Same structure viewed from an angle along the arrow shown in (A).
  The above figures are reprinted by permission from Cell Press: Cell (2000, 100, 551-560) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21139638 E.Schleiff, and T.Becker (2011).
Common ground for protein translocation: access control for mitochondria and chloroplasts.
  Nat Rev Mol Cell Biol, 12, 48-59.  
21173275 H.Yamamoto, N.Itoh, S.Kawano, Y.Yatsukawa, T.Momose, T.Makio, M.Matsunaga, M.Yokota, M.Esaki, T.Shodai, D.Kohda, A.E.Hobbs, R.E.Jensen, and T.Endo (2011).
Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.
  Proc Natl Acad Sci U S A, 108, 91-96.  
20504278 A.C.Fan, L.M.Gava, C.H.Ramos, and J.C.Young (2010).
Human mitochondrial import receptor Tom70 functions as a monomer.
  Biochem J, 429, 553-563.  
19595762 C.T.Chu (2010).
Tickled PINK1: mitochondrial homeostasis and autophagy in recessive Parkinsonism.
  Biochim Biophys Acta, 1802, 20-28.  
20442789 G.Domańska, C.Motz, M.Meinecke, A.Harsman, P.Papatheodorou, B.Reljic, E.A.Dian-Lothrop, A.Galmiche, O.Kepp, L.Becker, K.Günnewig, R.Wagner, and J.Rassow (2010).
Helicobacter pylori VacA toxin/subunit p34: targeting of an anion channel to the inner mitochondrial membrane.
  PLoS Pathog, 6, e1000878.  
21059946 L.Banci, I.Bertini, C.Cefaro, L.Cenacchi, S.Ciofi-Baffoni, I.C.Felli, A.Gallo, L.Gonnelli, E.Luchinat, D.Sideris, and K.Tokatlidis (2010).
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.
  Proc Natl Acad Sci U S A, 107, 20190-20195.
PDB code: 2l0y
20718036 la Cruz, R.Bajaj, S.Becker, and M.Zweckstetter (2010).
The intermembrane space domain of Tim23 is intrinsically disordered with a distinct binding region for presequences.
  Protein Sci, 19, 2045-2054.  
20680033 R.Lin, S.Paz, and J.Hiscott (2010).
Tom70 imports antiviral immunity to the mitochondria.
  Cell Res, 20, 971-973.  
20435646 W.Q.Li, X.Q.Zhang, C.Xia, Y.Deng, and D.Ye (2010).
MALE GAMETOPHYTE DEFECTIVE 1, encoding the FAd subunit of mitochondrial F1F0-ATP synthase, is essential for pollen formation in Arabidopsis thaliana.
  Plant Cell Physiol, 51, 923-935.  
20628368 X.Y.Liu, B.Wei, H.X.Shi, Y.F.Shan, and C.Wang (2010).
Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.
  Cell Res, 20, 994.  
21102411 Y.Sato, H.Shibata, T.Nakatsu, H.Nakano, Y.Kashiwayama, T.Imanaka, and H.Kato (2010).
Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p.
  EMBO J, 29, 4083-4093.
PDB code: 3ajb
19995731 A.K.Berglund, E.Spånning, H.Biverståhl, G.Maddalo, C.Tellgren-Roth, L.Mäler, and E.Glaser (2009).
Dual Targeting to Mitochondria and Chloroplasts: Characterization of Thr-tRNA Synthetase Targeting Peptide.
  Mol Plant, 2, 1298-1309.  
19754976 C.Desler, P.Suravajhala, M.Sanderhoff, M.Rasmussen, and L.J.Rasmussen (2009).
In Silico screening for functional candidates amongst hypothetical proteins.
  BMC Bioinformatics, 10, 289.  
20026652 D.P.Sideris, N.Petrakis, N.Katrakili, D.Mikropoulou, A.Gallo, S.Ciofi-Baffoni, L.Banci, I.Bertini, and K.Tokatlidis (2009).
A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding.
  J Cell Biol, 187, 1007-1022.  
19767391 H.Yamamoto, K.Fukui, H.Takahashi, S.Kitamura, T.Shiota, K.Terao, M.Uchida, M.Esaki, S.Nishikawa, T.Yoshihisa, K.Yamano, and T.Endo (2009).
Roles of Tom70 in import of presequence-containing mitochondrial proteins.
  J Biol Chem, 284, 31635-31646.  
19581297 J.Li, X.Qian, J.Hu, and B.Sha (2009).
Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.
  J Biol Chem, 284, 23852-23859.
PDB codes: 3fp2 3fp3 3fp4
19691130 R.Alag, N.Bharatham, A.Dong, T.Hills, A.Harikishore, A.A.Widjaja, S.G.Shochat, R.Hui, and H.S.Yoon (2009).
Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
  Protein Sci, 18, 2115-2124.
PDB code: 2fbn
19028997 R.F.Waller, C.Jabbour, N.C.Chan, N.Celik, V.A.Likic, T.D.Mulhern, and T.Lithgow (2009).
Evidence of a reduced and modified mitochondrial protein import apparatus in microsporidian mitosomes.
  Eukaryot Cell, 8, 19-26.  
19453276 T.Endo, and K.Yamano (2009).
Multiple pathways for mitochondrial protein traffic.
  Biol Chem, 390, 723-730.  
18369189 C.J.McCleverty, L.Columbus, A.Kreusch, and S.A.Lesley (2008).
Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.
  Protein Sci, 17, 869-877.
PDB codes: 2vkj 2vko
18537026 E.P.Neve, and M.Ingelman-Sundberg (2008).
Intracellular transport and localization of microsomal cytochrome P450.
  Anal Bioanal Chem, 392, 1075-1084.  
18551319 J.M.Kang, H.I.Cheun, J.Kim, S.U.Moon, S.J.Park, T.S.Kim, W.M.Sohn, and B.K.Na (2008).
Identification and characterization of a mitochondrial iron-superoxide dismutase of Cryptosporidium parvum.
  Parasitol Res, 103, 787-795.  
18063580 K.Yamano, Y.Yatsukawa, M.Esaki, A.E.Hobbs, R.E.Jensen, and T.Endo (2008).
Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import.
  J Biol Chem, 283, 3799-3807.  
18174896 N.Bolender, A.Sickmann, R.Wagner, C.Meisinger, and N.Pfanner (2008).
Multiple pathways for sorting mitochondrial precursor proteins.
  EMBO Rep, 9, 42-49.  
17696772 D.Milenkovic, J.Müller, D.Stojanovski, N.Pfanner, and A.Chacinska (2007).
Diverse mechanisms and machineries for import of mitochondrial proteins.
  Biol Chem, 388, 891-897.  
17391014 H.Xie, S.Vucetic, L.M.Iakoucheva, C.J.Oldfield, A.K.Dunker, V.N.Uversky, and Z.Obradovic (2007).
Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.
  J Proteome Res, 6, 1882-1898.  
18022369 I.Gelis, A.M.Bonvin, D.Keramisanou, M.Koukaki, G.Gouridis, S.Karamanou, A.Economou, and C.G.Kalodimos (2007).
Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.
  Cell, 131, 756-769.
PDB code: 2vda
17300922 J.A.MacKenzie, and R.M.Payne (2007).
Mitochondrial protein import and human health and disease.
  Biochim Biophys Acta, 1772, 509-523.  
17261588 L.E.Reddick, M.D.Vaughn, S.J.Wright, I.M.Campbell, and B.D.Bruce (2007).
In vitro comparative kinetic analysis of the chloroplast Toc GTPases.
  J Biol Chem, 282, 11410-11426.  
17825565 M.J.Baker, A.E.Frazier, J.M.Gulbis, and M.T.Ryan (2007).
Mitochondrial protein-import machinery: correlating structure with function.
  Trends Cell Biol, 17, 456-464.  
17596514 M.K.Bhangoo, S.Tzankov, A.C.Fan, K.Dejgaard, D.Y.Thomas, and J.C.Young (2007).
Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.
  Mol Biol Cell, 18, 3414-3428.  
17446895 O.Emanuelsson, S.Brunak, G.von Heijne, and H.Nielsen (2007).
Locating proteins in the cell using TargetP, SignalP and related tools.
  Nat Protoc, 2, 953-971.  
17998403 S.Kutik, B.Guiard, H.E.Meyer, N.Wiedemann, and N.Pfanner (2007).
Cooperation of translocase complexes in mitochondrial protein import.
  J Cell Biol, 179, 585-591.  
17948058 T.Saitoh, M.Igura, T.Obita, T.Ose, R.Kojima, K.Maenaka, T.Endo, and D.Kohda (2007).
Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states.
  EMBO J, 26, 4777-4787.
PDB codes: 2v1s 2v1t
17263664 W.Neupert, and J.M.Herrmann (2007).
Translocation of proteins into mitochondria.
  Annu Rev Biochem, 76, 723-749.  
17420252 Y.Abe, T.Jo, Y.Matsuda, C.Matsunaga, T.Katayama, and T.Ueda (2007).
Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC.
  J Biol Chem, 282, 17816-17827.
PDB code: 2e0g
17998537 Y.Zhang, and D.C.Chan (2007).
Structural basis for recruitment of mitochondrial fission complexes by Fis1.
  Proc Natl Acad Sci U S A, 104, 18526-18530.
PDB codes: 2pqn 2pqr
17008120 A.H.Millar, J.Whelan, and I.Small (2006).
Recent surprises in protein targeting to mitochondria and plastids.
  Curr Opin Plant Biol, 9, 610-615.  
16461275 A.J.Perry, J.M.Hulett, V.A.Likić, T.Lithgow, and P.R.Gooley (2006).
Convergent evolution of receptors for protein import into mitochondria.
  Curr Biol, 16, 221-229.
PDB code: 1zu2
17088320 A.Mukhopadhyay, C.S.Yang, and H.Weiner (2006).
Binding of mitochondrial leader sequences to Tom20 assessed using a bacterial two-hybrid system shows that hydrophobic interactions are essential and that some mutated leaders that do not bind Tom20 can still be imported.
  Protein Sci, 15, 2739-2748.  
16616497 Marcos-Lousa, D.P.Sideris, and K.Tokatlidis (2006).
Translocation of mitochondrial inner-membrane proteins: conformation matters.
  Trends Biochem Sci, 31, 259-267.  
16914527 J.M.Harper, M.H.Huynh, I.Coppens, F.Parussini, S.Moreno, and V.B.Carruthers (2006).
A cleavable propeptide influences Toxoplasma infection by facilitating the trafficking and secretion of the TgMIC2-M2AP invasion complex.
  Mol Biol Cell, 17, 4551-4563.  
16857931 P.Dolezal, V.Likic, J.Tachezy, and T.Lithgow (2006).
Evolution of the molecular machines for protein import into mitochondria.
  Science, 313, 314-318.  
17099692 R.Albrecht, P.Rehling, A.Chacinska, J.Brix, S.A.Cadamuro, R.Volkmer, B.Guiard, N.Pfanner, and K.Zeth (2006).
The Tim21 binding domain connects the preprotein translocases of both mitochondrial membranes.
  EMBO Rep, 7, 1233-1238.
PDB code: 2ciu
16546069 R.Lister, and J.Whelan (2006).
Mitochondrial protein import: convergent solutions for receptor structure.
  Curr Biol, 16, R197-R199.  
16892083 W.C.Cheng, S.B.Berman, I.Ivanovska, E.A.Jonas, S.J.Lee, Y.Chen, L.K.Kaczmarek, F.Pineda, and J.M.Hardwick (2006).
Mitochondrial factors with dual roles in death and survival.
  Oncogene, 25, 4697-4705.  
16767096 Y.Wu, and B.Sha (2006).
Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p.
  Nat Struct Mol Biol, 13, 589-593.
PDB code: 2gw1
16331427 A.J.Perry, J.M.Hulett, T.Lithgow, and P.R.Gooley (2005).
1H, 13C and 15N resonance assignments of the cytosolic domain of Tom20 from Arabidopsis thaliana.
  J Biomol NMR, 33, 198.  
15634341 C.G.Wilson, T.Kajander, and L.Regan (2005).
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
  FEBS J, 272, 166-179.
PDB code: 1xnf
15882268 I.Santamaría, D.Alvarez-Hernández, R.Jofré, J.R.Polo, J.Menárguez, and J.B.Cannata-Andía (2005).
Progression of secondary hyperparathyroidism involves deregulation of genes related to DNA and RNA stability.
  Kidney Int, 67, 2267-2279.  
  16511083 M.Igura, T.Ose, T.Obita, C.Sato, K.Maenaka, T.Endo, and D.Kohda (2005).
Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 514-517.  
15605252 X.Chen, R.P.Moerschell, D.A.Pearce, D.D.Ramanan, and F.Sherman (2005).
Enhanced mitochondrial degradation of yeast cytochrome c with amphipathic structures.
  Curr Genet, 47, 67-83.  
15473843 C.M.Koehler (2004).
New developments in mitochondrial assembly.
  Annu Rev Cell Dev Biol, 20, 309-335.  
15294046 D.A.Hood, and A.M.Joseph (2004).
Mitochondrial assembly: protein import.
  Proc Nutr Soc, 63, 293-300.  
15075277 J.Slapeta, and J.S.Keithly (2004).
Cryptosporidium parvum mitochondrial-type HSP70 targets homologous and heterologous mitochondria.
  Eukaryot Cell, 3, 483-494.  
15337763 M.Esaki, H.Shimizu, T.Ono, H.Yamamoto, T.Kanamori, S.Nishikawa, and T.Endo (2004).
Mitochondrial protein import. Requirement of presequence elements and tom components for precursor binding to the TOM complex.
  J Biol Chem, 279, 45701-45707.  
14699115 M.Yano, K.Terada, and M.Mori (2004).
Mitochondrial import receptors Tom20 and Tom22 have chaperone-like activity.
  J Biol Chem, 279, 10808-10813.  
15523480 N.Pfanner, N.Wiedemann, C.Meisinger, and T.Lithgow (2004).
Assembling the mitochondrial outer membrane.
  Nat Struct Mol Biol, 11, 1044-1048.  
14973134 N.Wiedemann, A.E.Frazier, and N.Pfanner (2004).
The protein import machinery of mitochondria.
  J Biol Chem, 279, 14473-14476.  
15232570 P.Rehling, K.Brandner, and N.Pfanner (2004).
Mitochondrial import and the twin-pore translocase.
  Nat Rev Mol Cell Biol, 5, 519-530.  
15215243 S.A.Graf, S.E.Haigh, E.D.Corson, and O.S.Shirihai (2004).
Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me).
  J Biol Chem, 279, 42954-42963.  
15316022 T.Beddoe, S.R.Bushell, M.A.Perugini, T.Lithgow, T.D.Mulhern, S.P.Bottomley, and J.Rossjohn (2004).
A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway.
  J Biol Chem, 279, 46448-46454.  
14985332 Y.Nakamura, H.Suzuki, M.Sakaguchi, and K.Mihara (2004).
Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex.
  J Biol Chem, 279, 21223-21232.  
14532110 A.Chacinska, P.Rehling, B.Guiard, A.E.Frazier, A.Schulze-Specking, N.Pfanner, W.Voos, and C.Meisinger (2003).
Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex.
  EMBO J, 22, 5370-5381.  
12660160 A.Yamashita, K.Maeda, and Y.Maéda (2003).
Crystal structure of CapZ: structural basis for actin filament barbed end capping.
  EMBO J, 22, 1529-1538.
PDB code: 1izn
14557549 K.J.Walters, P.J.Lech, A.M.Goh, Q.Wang, and P.M.Howley (2003).
DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a.
  Proc Natl Acad Sci U S A, 100, 12694-12699.
PDB codes: 1oqy 1qze
12899691 M.San Miguel, R.Marrington, P.M.Rodger, A.Rodger, and C.Robinson (2003).
An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment.
  Eur J Biochem, 270, 3345-3352.  
14557246 M.Yano, K.Terada, and M.Mori (2003).
AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins.
  J Cell Biol, 163, 45-56.  
12556518 M.von und zu Fraunberg, T.Nyröen, and R.Kauppinen (2003).
Mitochondrial targeting of normal and mutant protoporphyrinogen oxidase.
  J Biol Chem, 278, 13376-13381.  
14617063 P.Moberg, A.Ståhl, S.Bhushan, S.J.Wright, A.Eriksson, B.D.Bruce, and E.Glaser (2003).
Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts.
  Plant J, 36, 616-628.  
12514182 T.Beilharz, B.Egan, P.A.Silver, K.Hofmann, and T.Lithgow (2003).
Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae.
  J Biol Chem, 278, 8219-8223.  
12640110 T.Stan, J.Brix, J.Schneider-Mergener, N.Pfanner, W.Neupert, and D.Rapaport (2003).
Mitochondrial protein import: recognition of internal import signals of BCS1 by the TOM complex.
  Mol Cell Biol, 23, 2239-2250.  
11877417 A.Brinker, C.Scheufler, F.Von Der Mulbe, B.Fleckenstein, C.Herrmann, G.Jung, I.Moarefi, and F.U.Hartl (2002).
Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.
  J Biol Chem, 277, 19265-19275.  
12185844 A.Chacinska, N.Pfanner, and C.Meisinger (2002).
How mitochondria import hydrophilic and hydrophobic proteins.
  Trends Cell Biol, 12, 299-303.  
12198123 A.J.Johnston, J.Hoogenraad, D.A.Dougan, K.N.Truscott, M.Yano, M.Mori, N.J.Hoogenraad, and M.T.Ryan (2002).
Insertion and assembly of human tom7 into the preprotein translocase complex of the outer mitochondrial membrane.
  J Biol Chem, 277, 42197-42204.  
11967360 A.Mukhopadhyay, P.Hammen, M.Waltner-Law, and H.Weiner (2002).
Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP).
  Protein Sci, 11, 1026-1035.  
12186850 B.Schwer, B.J.North, R.A.Frye, M.Ott, and E.Verdin (2002).
The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase.
  J Cell Biol, 158, 647-657.  
12000457 C.Rudhe, O.Chew, J.Whelan, and E.Glaser (2002).
A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts.
  Plant J, 30, 213-220.  
11986670 H.Bose, V.R.Lingappa, and W.L.Miller (2002).
Rapid regulation of steroidogenesis by mitochondrial protein import.
  Nature, 417, 87-91.  
12383789 N.Pfanner, and N.Wiedemann (2002).
Mitochondrial protein import: two membranes, three translocases.
  Curr Opin Cell Biol, 14, 400-411.  
  12653482 N.Plesofsky, and R.Brambl (2002).
Analysis of interactions between domains of a small heat shock protein, Hsp30 of Neurospora crassa.
  Cell Stress Chaperones, 7, 374-386.  
11684692 R.D.Moir, K.V.Puglia, and I.M.Willis (2002).
Autoinhibition of TFIIIB70 binding by the tetratricopeptide repeat-containing subunit of TFIIIC.
  J Biol Chem, 277, 694-701.  
12167707 R.D.Moir, K.V.Puglia, and I.M.Willis (2002).
A gain-of-function mutation in the second tetratricopeptide repeat of TFIIIC131 relieves autoinhibition of Brf1 binding.
  Mol Cell Biol, 22, 6131-6141.  
11887183 S.Huang, K.S.Ratliff, and A.Matouschek (2002).
Protein unfolding by the mitochondrial membrane potential.
  Nat Struct Biol, 9, 301-307.  
12138093 S.Vial, H.Lu, S.Allen, P.Savory, D.Thornton, J.Sheehan, and K.Tokatlidis (2002).
Assembly of Tim9 and Tim10 into a functional chaperone.
  J Biol Chem, 277, 36100-36108.  
11208169 B.Wattenberg, and T.Lithgow (2001).
Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes.
  Traffic, 2, 66-71.  
11576437 G.Duby, M.Oufattole, and M.Boutry (2001).
Hydrophobic residues within the predicted N-terminal amphiphilic alpha-helix of a plant mitochondrial targeting presequence play a major role in in vivo import.
  Plant J, 27, 539-549.  
11604494 J.Y.Koh, P.Hájek, and D.M.Bedwell (2001).
Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae.
  Mol Cell Biol, 21, 7576-7586.  
11137038 M.Chinkers (2001).
Protein phosphatase 5 in signal transduction.
  Trends Endocrinol Metab, 12, 28-32.  
11828482 T.Krimmer, A.Geissler, N.Pfanner, and J.Rassow (2001).
Sorting of preproteins into mitochondria.
  Chembiochem, 2, 505-512.  
11567104 X.J.Morelli, P.N.Palma, F.Guerlesquin, and A.C.Rigby (2001).
A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.
  Protein Sci, 10, 2131-2137.  
11576427 X.P.Zhang, S.Sjöling, M.Tanudji, L.Somogyi, D.Andreu, L.E.Eriksson, A.Gräslund, J.Whelan, and E.Glaser (2001).
Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase.
  Plant J, 27, 427-438.  
10943834 D.W.Andrews (2000).
Transport across membranes: a question of navigation.
  Cell, 102, 139-144.  
10982837 M.Yano, N.Hoogenraad, K.Terada, and M.Mori (2000).
Identification and functional analysis of human Tom22 for protein import into mitochondria.
  Mol Cell Biol, 20, 7205-7213.  
10837244 N.Pfanner (2000).
Protein sorting: recognizing mitochondrial presequences.
  Curr Biol, 10, R412-R415.  
10990453 T.Stan, U.Ahting, M.Dembowski, K.P.Künkele, S.Nussberger, W.Neupert, and D.Rapaport (2000).
Recognition of preproteins by the isolated TOM complex of mitochondria.
  EMBO J, 19, 4895-4902.  
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.