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3uux
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of yeast Fis1 in complex with Mdv1 fragment containing N-terminal extension and coiled coil domains== | |
| + | <StructureSection load='3uux' size='340' side='right'caption='[[3uux]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3uux]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UUX 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;'>[[2pqn|2pqn]], [[2pqr|2pqr]], [[2xu6|2xu6]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FIS1, MDV2, YIL065C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), MDV1, FIS2, GAG3, NET2, YJL112W, J0802 ([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=3uux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uux OCA], [https://pdbe.org/3uux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uux RCSB], [https://www.ebi.ac.uk/pdbsum/3uux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uux ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitochondrial fission machinery is best understood in the yeast Saccharomyces cerevisiae, where Fis1, Mdv1, and Dnm1 are essential components. Fis1 is a mitochondrial outer membrane protein that recruits the dynamin-related GTPase Dnm1 during the fission process. This recruitment occurs via Mdv1, which binds both Fis1 and Dnm1 and therefore functions as a molecular adaptor linking the two molecules. Mdv1 has a modular structure, consisting of an N-terminal extension that binds Fis1, a central coiled coil for dimerization, and a C-terminal WD40 repeat region that binds Dnm1. We have solved the crystal structure of a dimeric Mdv1-Fis1 complex that contains both the N-terminal extension and coiled-coil regions of Mdv1. Consistent with previous studies, Mdv1 binds Fis1 through a U-shaped helix-loop-helix motif, and dimerization of the Mdv1-Fis1 complex is mediated by the antiparallel coiled coil of Mdv1. However, the complex is surprisingly compact and rigid due to two additional contacts mediated by the surface of the Mdv1 coiled coil. The coiled coil packs against both Fis1 and the second helix of the Mdv1 helix-loop-helix motif. Mutational analyses showed that these contacts are important for mitochondrial fission activity. These results indicate that, in addition to dimerization, the unusually long Mdv1 coiled coil serves a scaffolding function to stabilize the Mdv1-Fis1 complex. | ||
| - | + | Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (mdv1) coiled coil.,Zhang Y, Chan NC, Ngo HB, Gristick H, Chan DC J Biol Chem. 2012 Mar 23;287(13):9855-61. Epub 2012 Feb 1. PMID:22303011<ref>PMID:22303011</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3uux" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chan, D C]] | ||
| + | [[Category: Chan, N C]] | ||
| + | [[Category: Gristick, H]] | ||
| + | [[Category: Zhang, Y]] | ||
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Mitochondria and cytoplasm]] | ||
| + | [[Category: Mitochondrial fission]] | ||
| + | [[Category: Tetratricopeptide repeat]] | ||
Current revision
Crystal structure of yeast Fis1 in complex with Mdv1 fragment containing N-terminal extension and coiled coil domains
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