5x9b

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Current revision (10:17, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5x9b' size='340' side='right'caption='[[5x9b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='5x9b' size='340' side='right'caption='[[5x9b]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X9B FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9c|5x9c]]</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]] 2.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MID51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5x9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9b OCA], [https://pdbe.org/5x9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x9b RCSB], [https://www.ebi.ac.uk/pdbsum/5x9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9b 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=5x9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9b OCA], [http://pdbe.org/5x9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9b RCSB], [http://www.ebi.ac.uk/pdbsum/5x9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9b ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MID51_HUMAN MID51_HUMAN]] 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.<ref>PMID:21508961</ref> <ref>PMID:21701560</ref> <ref>PMID:23921378</ref> <ref>PMID:23283981</ref> <ref>PMID:23530241</ref>
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[https://www.uniprot.org/uniprot/MID51_HUMAN MID51_HUMAN] 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.<ref>PMID:21508961</ref> <ref>PMID:21701560</ref> <ref>PMID:23921378</ref> <ref>PMID:23283981</ref> <ref>PMID:23530241</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mitochondrial fission is facilitated by dynamin-related protein Drp1 and a variety of its receptors. However, the molecular mechanism of how Drp1 is recruited to the mitochondrial surface by receptors MiD49 and MiD51 remains elusive. Here, we showed that the interaction between Drp1 and MiD51 is regulated by GTP binding and depends on the polymerization of Drp1. We identified two regions on MiD51 that directly bind to Drp1, and found that dimerization of MiD51, relevant to residue C452, is required for mitochondrial dynamics regulation. Our Results have suggested a multi-faceted regulatory mechanism for the interaction between Drp1 and MiD51 that illustrates the potentially complicated and tight regulation of mitochondrial fission.
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New interfaces on MiD51 for Drp1 recruitment and regulation.,Ma J, Zhai Y, Chen M, Zhang K, Chen Q, Pang X, Sun F PLoS One. 2019 Jan 31;14(1):e0211459. doi: 10.1371/journal.pone.0211459., eCollection 2019. PMID:30703167<ref>PMID:30703167</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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<div class="pdbe-citations 5x9b" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ma, J]]
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[[Category: Ma J]]
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[[Category: Pang, X]]
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[[Category: Pang X]]
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[[Category: Sun, F]]
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[[Category: Sun F]]
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[[Category: Mitochondrial fission]]
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[[Category: Nucleotidyltransferase fold]]
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[[Category: Receptor]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the cytosolic domain of human MiD51

PDB ID 5x9b

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Proteopedia Page Contributors and Editors (what is this?)

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