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| | <StructureSection load='4woy' size='340' side='right'caption='[[4woy]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4woy' size='340' side='right'caption='[[4woy]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4woy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WOY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4woy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WOY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wp0|4wp0]]</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mief2, Gm11, Mid49, Smcr7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4woy OCA], [https://pdbe.org/4woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4woy RCSB], [https://www.ebi.ac.uk/pdbsum/4woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4woy 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=4woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4woy OCA], [http://pdbe.org/4woy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4woy RCSB], [http://www.ebi.ac.uk/pdbsum/4woy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4woy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MID49_MOUSE MID49_MOUSE]] Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity.<ref>PMID:23283981</ref> <ref>PMID:24508339</ref> | + | [https://www.uniprot.org/uniprot/MID49_MOUSE MID49_MOUSE] Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity.<ref>PMID:23283981</ref> <ref>PMID:24508339</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chan, D C]] | + | [[Category: Chan DC]] |
| - | [[Category: Kaiser, J T]] | + | [[Category: Kaiser JT]] |
| - | [[Category: Liu, R]] | + | [[Category: Liu R]] |
| - | [[Category: Loson, O C]] | + | [[Category: Loson OC]] |
| - | [[Category: Meng, S]] | + | [[Category: Meng S]] |
| - | [[Category: Ngo, H B]] | + | [[Category: Ngo HB]] |
| - | [[Category: Mid49]]
| + | |
| - | [[Category: Mitochondrial fission]]
| + | |
| - | [[Category: Nucleotidyl transferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
MID49_MOUSE Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity.[1] [2]
Publication Abstract from PubMed
Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface, where assembly leads to activation of its GTP-dependent scission function. MiD49 and MiD51 are two receptors on the mitochondrial outer membrane that can recruit Drp1 to facilitate mitochondrial fission. Structural studies indicated that MiD51 has a variant nucleotidyl transferase fold that binds an ADP co-factor essential for activation of Drp1 function. MiD49 shares sequence homology with MiD51 and regulates Drp1 function. However, it is unknown if MiD49 binds an analogous co-factor. Because MiD49 does not readily crystallize, we used structural predictions and biochemical screening to identify a surface entropy reduction mutant that facilitated crystallization. Using molecular replacement, we determined the atomic structure of MiD49 to 2.4 A. Like MiD51, MiD49 contains a nucleotidyl transferase domain; however, the electron density provides no evidence for a small-molecule ligand. Structural changes in the putative nucleotide-binding pocket make MiD49 incompatible with an extended ligand like ADP, and critical nucleotide-binding residues found in MiD51 are not conserved. MiD49 contains a surface loop that physically interacts with Drp1 and is necessary for Drp1 recruitment to the mitochondrial surface. Our results suggest a structural basis for the differential regulation of MiD51- versus MiD49-mediated fission. This article is protected by copyright. All rights reserved.
Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1.,Losomicronn OC, Meng S, Ngo H, Liu R, Kaiser JT, Chan DC Protein Sci. 2015 Jan 10. doi: 10.1002/pro.2629. PMID:25581164[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Loson OC, Song Z, Chen H, Chan DC. Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol Biol Cell. 2013 Mar;24(5):659-67. doi: 10.1091/mbc.E12-10-0721. Epub 2013 Jan, 2. PMID:23283981 doi:http://dx.doi.org/10.1091/mbc.E12-10-0721
- ↑ Loson OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC. The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor. Structure. 2014 Mar 4;22(3):367-77. doi: 10.1016/j.str.2014.01.001. Epub 2014 Feb, 6. PMID:24508339 doi:http://dx.doi.org/10.1016/j.str.2014.01.001
- ↑ Losomicronn OC, Meng S, Ngo H, Liu R, Kaiser JT, Chan DC. Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1. Protein Sci. 2015 Jan 10. doi: 10.1002/pro.2629. PMID:25581164 doi:http://dx.doi.org/10.1002/pro.2629
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