4oah

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==Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant==
==Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant==
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<StructureSection load='4oah' size='340' side='right' caption='[[4oah]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4oah' size='340' side='right'caption='[[4oah]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4oah]] is a 4 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=4OAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OAH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4oah]] is a 4 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=4OAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OAH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oaf|4oaf]], [[4oag|4oag]], [[4oai|4oai]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mid51, MiD51 (aka SMCR7L), Mief1, Smcr7l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4oah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oah OCA], [https://pdbe.org/4oah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oah RCSB], [https://www.ebi.ac.uk/pdbsum/4oah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oah ProSAT]</span></td></tr>
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<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=4oah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oah RCSB], [http://www.ebi.ac.uk/pdbsum/4oah PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MID51_MOUSE MID51_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.
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[https://www.uniprot.org/uniprot/MID51_MOUSE MID51_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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface and activation of its GTP-dependent scission function. The Drp1 receptors MiD49 and MiD51 recruit Drp1 to facilitate mitochondrial fission, but their mechanism of action is poorly understood. Using X-ray crystallography, we demonstrate that MiD51 contains a nucleotidyl transferase domain that binds ADP with high affinity. MiD51 recruits Drp1 via a surface loop that functions independently of ADP binding. However, in the absence of nucleotide binding, the recruited Drp1 cannot be activated for fission. Purified MiD51 strongly inhibits Drp1 assembly and GTP hydrolysis in the absence of ADP. Addition of ADP relieves this inhibition and promotes Drp1 assembly into spirals with enhanced GTP hydrolysis. Our results reveal ADP as an essential cofactor for MiD51 during mitochondrial fission.
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The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor.,Loson OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC Structure. 2014 Mar 4;22(3):367-77. doi: 10.1016/j.str.2014.01.001. Epub 2014 Feb, 6. PMID:24508339<ref>PMID:24508339</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Chan, D C]]
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[[Category: Mus musculus]]
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[[Category: Kaiser, J T]]
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[[Category: Chan DC]]
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[[Category: Loson, O C]]
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[[Category: Kaiser JT]]
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[[Category: Nucleotidyl transferase fold]]
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[[Category: Loson OC]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant

PDB ID 4oah

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