5x9c: Difference between revisions

Latest revision as of 07:56, 22 November 2023

Crystal structure of the cytosolic domain of human MiD51

Structural highlights

5x9c is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT. MiD49 and MiD51, new components of the mitochondrial fission machinery. EMBO Rep. 2011 Jun;12(6):565-73. doi: 10.1038/embor.2011.54. Epub 2011 Apr 21. PMID:21508961 doi:https://dx.doi.org/10.1038/embor.2011.54
↑ Zhao J, Liu T, Jin S, Wang X, Qu M, Uhlen P, Tomilin N, Shupliakov O, Lendahl U, Nister M. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 2011 Jun 24;30(14):2762-78. doi: 10.1038/emboj.2011.198. PMID:21701560 doi:https://dx.doi.org/10.1038/emboj.2011.198
↑ Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT. Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission. J Biol Chem. 2013 Sep 20;288(38):27584-93. doi: 10.1074/jbc.M113.479873. Epub, 2013 Aug 6. PMID:23921378 doi:https://dx.doi.org/10.1074/jbc.M113.479873
↑ 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:https://dx.doi.org/10.1091/mbc.E12-10-0721
↑ Koirala S, Guo Q, Kalia R, Bui HT, Eckert DM, Frost A, Shaw JM. Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):E1342-51. doi:, 10.1073/pnas.1300855110. Epub 2013 Mar 25. PMID:23530241 doi:https://dx.doi.org/10.1073/pnas.1300855110

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OCA

[1] Palmer CS, Osellame LD, Laine D, Koutsopoulos OS, Frazier AE, Ryan MT. MiD49 and MiD51, new components of the mitochondrial fission machinery. EMBO Rep. 2011 Jun;12(6):565-73. doi: 10.1038/embor.2011.54. Epub 2011 Apr 21. PMID:21508961 doi:https://dx.doi.org/10.1038/embor.2011.54

[2] Zhao J, Liu T, Jin S, Wang X, Qu M, Uhlen P, Tomilin N, Shupliakov O, Lendahl U, Nister M. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 2011 Jun 24;30(14):2762-78. doi: 10.1038/emboj.2011.198. PMID:21701560 doi:https://dx.doi.org/10.1038/emboj.2011.198

[3] Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT. Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission. J Biol Chem. 2013 Sep 20;288(38):27584-93. doi: 10.1074/jbc.M113.479873. Epub, 2013 Aug 6. PMID:23921378 doi:https://dx.doi.org/10.1074/jbc.M113.479873

[4] 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:https://dx.doi.org/10.1091/mbc.E12-10-0721

[5] Koirala S, Guo Q, Kalia R, Bui HT, Eckert DM, Frost A, Shaw JM. Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission. Proc Natl Acad Sci U S A. 2013 Apr 9;110(15):E1342-51. doi:, 10.1073/pnas.1300855110. Epub 2013 Mar 25. PMID:23530241 doi:https://dx.doi.org/10.1073/pnas.1300855110

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[2]

[3]

[4]

[5]

@@ Line 3: / Line 3: @@
 <StructureSection load='5x9c' size='340' side='right'caption='[[5x9c]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5x9c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X9C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5x9c]] is a 2 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=5X9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X9C FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9b|5x9b]]</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]] 1.85&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9c OCA], [http://pdbe.org/5x9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9c RCSB], [http://www.ebi.ac.uk/pdbsum/5x9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9c ProSAT]</span></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=5x9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9c OCA], [https://pdbe.org/5x9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x9c RCSB], [https://www.ebi.ac.uk/pdbsum/5x9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9c ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ma, J]]
+[[Category: Ma J]]
-[[Category: Pang, X]]
+[[Category: Pang X]]
-[[Category: Sun, F]]
+[[Category: Sun F]]
-[[Category: Mitochondrial fission]]
-[[Category: Nucleotidyltransferase fold]]
-[[Category: Receptor]]
-[[Category: Transferase]]

5x9c: Difference between revisions

Latest revision as of 07:56, 22 November 2023

Crystal structure of the cytosolic domain of human MiD51

Structural highlights

Function

References

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