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< | ==CRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEX== | ||
<StructureSection load='2v1t' size='340' side='right'caption='[[2v1t]], [[Resolution|resolution]] 1.92Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v1t]] is a 4 chain structure with sequence from [https://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=1wt4 1wt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1T 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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
-- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1om2|1om2]], [[1wt4|1wt4]], [[2cuv|2cuv]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(+)) Aldehyde dehydrogenase (NAD(+))], with EC number [https://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=2v1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1t OCA], [https://pdbe.org/2v1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1t RCSB], [https://www.ebi.ac.uk/pdbsum/2v1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1t ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/2v1t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v1t ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:17948058</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2v1t" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Endo, T | __TOC__ | ||
[[Category: Igura, M | </StructureSection> | ||
[[Category: Kohda, D | [[Category: Buffalo rat]] | ||
[[Category: Maenaka, K | [[Category: Large Structures]] | ||
[[Category: Obita, T | [[Category: Endo, T]] | ||
[[Category: Ose, T | [[Category: Igura, M]] | ||
[[Category: Kohda, D]] | |||
[[Category: Maenaka, K]] | |||
[[Category: Obita, T]] | |||
[[Category: Ose, T]] | |||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Mitochondrion]] | [[Category: Mitochondrion]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Phosphorylation]] | [[Category: Phosphorylation]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
[[Category: Transit peptide]] | [[Category: Transit peptide]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
Latest revision as of 15:36, 23 March 2022
CRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEXCRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEX
Structural highlights
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 PubMedMost 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 |
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