| Structural highlights
4nxu is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 4nxt, 4nxv, 4nxw, 4nxx |
| Gene: | candidate 7-like, MID51, MIEF1, SMCR7L, Smith-Magenis syndrome chromosome region (HUMAN) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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]
Publication Abstract from PubMed
Mitochondrial fission is important for organelle transport, inheritance, and turnover, and alterations in fission are seen in neurological disease. In mammals, mitochondrial fission is executed by dynamin-related protein 1 (Drp1), a cytosolic guanosine triphosphatase that polymerizes and constricts the organelle. Recruitment of Drp1 to mitochondria involves receptors including Mff, MiD49, and MiD51. MiD49/51 form foci at mitochondrial constriction sites and coassemble with Drp1 to drive fission. Here, we solved the crystal structure of the cytosolic domain of human MiD51, which adopts a nucleotidyltransferase fold. Although MiD51 lacks catalytic residues for transferase activity, it specifically binds guanosine diphosphate and adenosine diphosphate. MiD51 mutants unable to bind nucleotides were still able to recruit Drp1. Disruption of an additional region in MiD51 that is not part of the nucleotidyltransferase fold blocked Drp1 recruitment and assembly of MiD51 into foci. MiD51 foci are also dependent on the presence of Drp1, and after scission they are distributed to daughter organelles, supporting the involvement of MiD51 in the fission apparatus.
Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission.,Richter V, Palmer CS, Osellame LD, Singh AP, Elgass K, Stroud DA, Sesaki H, Kvansakul M, Ryan MT J Cell Biol. 2014 Feb 17;204(4):477-86. doi: 10.1083/jcb.201311014. Epub 2014 Feb, 10. PMID:24515348[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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:http://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:http://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:http://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:http://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:http://dx.doi.org/10.1073/pnas.1300855110
- ↑ Richter V, Palmer CS, Osellame LD, Singh AP, Elgass K, Stroud DA, Sesaki H, Kvansakul M, Ryan MT. Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission. J Cell Biol. 2014 Feb 17;204(4):477-86. doi: 10.1083/jcb.201311014. Epub 2014 Feb, 10. PMID:24515348 doi:http://dx.doi.org/10.1083/jcb.201311014
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