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| | <StructureSection load='2pqn' size='340' side='right'caption='[[2pqn]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='2pqn' size='340' side='right'caption='[[2pqn]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pqn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pqn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQN 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;'>[[2pqr|2pqr]]</div></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]] 2.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FIS1, MDV2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), MDV1, FIS2, GAG3, NET2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqn OCA], [https://pdbe.org/2pqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqn RCSB], [https://www.ebi.ac.uk/pdbsum/2pqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqn ProSAT]</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=2pqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqn OCA], [https://pdbe.org/2pqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqn RCSB], [https://www.ebi.ac.uk/pdbsum/2pqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FIS1_YEAST FIS1_YEAST]] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.<ref>PMID:11038183</ref> <ref>PMID:11038182</ref> <ref>PMID:12163467</ref> <ref>PMID:12679388</ref> [[https://www.uniprot.org/uniprot/MDV1_YEAST MDV1_YEAST]] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.<ref>PMID:11038182</ref> <ref>PMID:11038180</ref> <ref>PMID:11038183</ref> <ref>PMID:12163467</ref> <ref>PMID:16247028</ref> <ref>PMID:16272155</ref> <ref>PMID:16601120</ref>
| + | [https://www.uniprot.org/uniprot/FIS1_YEAST FIS1_YEAST] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.<ref>PMID:11038183</ref> <ref>PMID:11038182</ref> <ref>PMID:12163467</ref> <ref>PMID:12679388</ref> |
| | == 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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chan, D C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Chan DC]] |
| - | [[Category: Apoptosis]] | + | [[Category: Zhang Y]] |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Tpr domain]]
| + | |
| Structural highlights
Function
FIS1_YEAST Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.[1] [2] [3] [4]
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
Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using crystallographic analysis of adaptor-Fis1 complexes, we show that these adaptors use two helices to bind to both the concave and convex surfaces of the Fis1 TPR domain. Fis1 therefore contains two interaction interfaces, a binding mode that, to our knowledge, has not been observed previously for TPR domains. Genetic and biochemical studies indicate that both binding interfaces are important for binding of Mdv1 and Caf4 to Fis1 and for mitochondrial fission activity in vivo. Our results reveal how Fis1 recruits the mitochondrial fission complex and will facilitate efforts to manipulate mitochondrial fission.
Structural basis for recruitment of mitochondrial fission complexes by Fis1.,Zhang Y, Chan DC Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000 Oct 16;151(2):367-80. PMID:11038183
- ↑ Tieu Q, Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J Cell Biol. 2000 Oct 16;151(2):353-66. PMID:11038182
- ↑ Tieu Q, Okreglak V, Naylor K, Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002 Aug 5;158(3):445-52. Epub 2002 Aug 5. PMID:12163467 doi:http://dx.doi.org/10.1083/jcb.200205031
- ↑ Jakobs S, Martini N, Schauss AC, Egner A, Westermann B, Hell SW. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J Cell Sci. 2003 May 15;116(Pt 10):2005-14. Epub 2003 Apr 1. PMID:12679388 doi:http://dx.doi.org/10.1242/jcs.00423
- ↑ Zhang Y, Chan DC. Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537
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