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| | ==CRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEX== | | ==CRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEX== |
| - | <StructureSection load='2v1s' size='340' side='right' caption='[[2v1s]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='2v1s' size='340' side='right'caption='[[2v1s]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v1s]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cuv 2cuv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V1S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v1s]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cuv 2cuv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1S FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CY3:2-AMINO-3-MERCAPTO-PROPIONAMIDE'>CY3</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1om2|1om2]], [[1wt4|1wt4]], [[2cuv|2cuv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CY3:2-AMINO-3-MERCAPTO-PROPIONAMIDE'>CY3</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(+)) Aldehyde dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.3 1.2.1.3] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1s OCA], [https://pdbe.org/2v1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1s RCSB], [https://www.ebi.ac.uk/pdbsum/2v1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1s OCA], [http://pdbe.org/2v1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v1s RCSB], [http://www.ebi.ac.uk/pdbsum/2v1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TOM20_RAT TOM20_RAT] Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Endo, T]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Igura, M]] | + | [[Category: Endo T]] |
| - | [[Category: Kohda, D]] | + | [[Category: Igura M]] |
| - | [[Category: Maenaka, K]] | + | [[Category: Kohda D]] |
| - | [[Category: Obita, T]] | + | [[Category: Maenaka K]] |
| - | [[Category: Ose, T]] | + | [[Category: Obita T]] |
| - | [[Category: Disulfide-bond tethering]]
| + | [[Category: Ose T]] |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Lipid synthesis]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein/oxidoreductase]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Outer membrane]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Steroid biosynthesis]]
| + | |
| - | [[Category: Sterol biosynthesis]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
TOM20_RAT Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Most mitochondrial proteins are synthesized in the cytosol and imported into mitochondria. The N-terminal presequences of mitochondrial-precursor proteins contain a diverse consensus motif (phi chi chi phi phi, phi is hydrophobic and chi is any amino acid), which is recognized by the Tom20 protein on the mitochondrial surface. To reveal the structural basis of the broad selectivity of Tom20, the Tom20-presequence complex was crystallized. Tethering a presequence peptide to Tom20 through a disulfide bond was essential for crystallization. Unexpectedly, the two crystals with different linker designs provided unique relative orientations of the presequence with respect to Tom20, and neither configuration could fully account for the hydrophobic preference at the three hydrophobic positions of the consensus motif. We propose the existence of a dynamic equilibrium in solution among multiple states including the two bound states. In accordance, NMR 15N relaxation analyses suggested motion on a sub-millisecond timescale at the Tom20-presequence interface. We suggest that the dynamic, multiple-mode interaction is the molecular mechanism facilitating the broadly selective specificity of the Tom20 receptor toward diverse mitochondrial presequences.
Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states.,Saitoh T, Igura M, Obita T, Ose T, Kojima R, Maenaka K, Endo T, Kohda D EMBO J. 2007 Nov 14;26(22):4777-87. Epub 2007 Oct 18. PMID:17948058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Saitoh T, Igura M, Obita T, Ose T, Kojima R, Maenaka K, Endo T, Kohda D. Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states. EMBO J. 2007 Nov 14;26(22):4777-87. Epub 2007 Oct 18. PMID:17948058 doi:7601888
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