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==Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1==
<StructureSection load='4woy' size='340' side='right'caption='[[4woy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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>
</table>
== Function ==
[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;">
== 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<ref>PMID:25581164</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4woy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Chan DC]]
[[Category: Kaiser JT]]
[[Category: Liu R]]
[[Category: Loson OC]]
[[Category: Meng S]]
[[Category: Ngo HB]]