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| | ==Solution structure of the ims domain of the mitochondrial import protein TIM21 from S. cerevisiae== | | ==Solution structure of the ims domain of the mitochondrial import protein TIM21 from S. cerevisiae== |
| - | <StructureSection load='2mf7' size='340' side='right'caption='[[2mf7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mf7' size='340' side='right'caption='[[2mf7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mf7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mf7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ciu|2ciu]]</div></td></tr> | + | </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=2mf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf7 OCA], [https://pdbe.org/2mf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf7 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIM21, YGR033C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=2mf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf7 OCA], [https://pdbe.org/2mf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf7 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TIM21_YEAST TIM21_YEAST]] Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex.<ref>PMID:15797382</ref> <ref>PMID:15878866</ref>
| + | [https://www.uniprot.org/uniprot/TIM21_YEAST TIM21_YEAST] Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex.<ref>PMID:15797382</ref> <ref>PMID:15878866</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bajaj, R]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Becker, S]] | + | [[Category: Bajaj R]] |
| - | [[Category: Jaremko, L]] | + | [[Category: Becker S]] |
| - | [[Category: Jaremko, M]] | + | [[Category: Jaremko L]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Jaremko M]] |
| - | [[Category: Ims domain]]
| + | [[Category: Zweckstetter M]] |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Mitochondrial import protein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Translocation]]
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| Structural highlights
Function
TIM21_YEAST Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex.[1] [2]
Publication Abstract from PubMed
The presequence translocase TIM23 is a highly dynamic complex in which its subunits can adopt multiple conformations and undergo association-dissociation to facilitate import of proteins into mitochondria. Despite the importance of protein-protein interactions in TIM23, little is known about the molecular details of these processes. Using nuclear magnetic resonance spectroscopy, we characterized the dynamic interaction network of the intermembrane space domains of Tim23, Tim21, Tim50, and Tom22 at single-residue level. We show that Tim23(IMS) contains multiple sites to efficiently interact with the intermembrane space domain of Tim21 and to bind to Tim21, Tim50, and Tom22. In addition, we reveal the atomic details of the dynamic Tim23(IMS)-Tim21(IMS) complex. The combined data support a central role of the intermembrane space domain of Tim23 in the formation and regulation of the presequence translocase.
Molecular Basis of the Dynamic Structure of the TIM23 Complex in the Mitochondrial Intermembrane Space.,Bajaj R, Jaremko L, Jaremko M, Becker S, Zweckstetter M Structure. 2014 Oct 7;22(10):1501-11. doi: 10.1016/j.str.2014.07.015. Epub 2014, Sep 25. PMID:25263020[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chacinska A, Lind M, Frazier AE, Dudek J, Meisinger C, Geissler A, Sickmann A, Meyer HE, Truscott KN, Guiard B, Pfanner N, Rehling P. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell. 2005 Mar 25;120(6):817-29. PMID:15797382 doi:http://dx.doi.org/10.1016/j.cell.2005.01.011
- ↑ Mokranjac D, Popov-Celeketic D, Hell K, Neupert W. Role of Tim21 in mitochondrial translocation contact sites. J Biol Chem. 2005 Jun 24;280(25):23437-40. Epub 2005 May 4. PMID:15878866 doi:http://dx.doi.org/C500135200
- ↑ Bajaj R, Jaremko L, Jaremko M, Becker S, Zweckstetter M. Molecular Basis of the Dynamic Structure of the TIM23 Complex in the Mitochondrial Intermembrane Space. Structure. 2014 Oct 7;22(10):1501-11. doi: 10.1016/j.str.2014.07.015. Epub 2014, Sep 25. PMID:25263020 doi:http://dx.doi.org/10.1016/j.str.2014.07.015
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