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| | <StructureSection load='5yk7' size='340' side='right'caption='[[5yk7]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='5yk7' size='340' side='right'caption='[[5yk7]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yk7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YK7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YK7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yk7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Zygosaccharomyces_rouxii_CBS_732 Zygosaccharomyces rouxii CBS 732]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YK7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 3.799Å</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=5yk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yk7 OCA], [http://pdbe.org/5yk7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yk7 RCSB], [http://www.ebi.ac.uk/pdbsum/5yk7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yk7 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5yk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yk7 OCA], [https://pdbe.org/5yk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yk7 RCSB], [https://www.ebi.ac.uk/pdbsum/5yk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yk7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MMM1_ZYGRC MMM1_ZYGRC]] Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. [[http://www.uniprot.org/uniprot/MDM12_YEAST MDM12_YEAST]] Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.[HAMAP-Rule:MF_03104]<ref>PMID:17410204</ref> <ref>PMID:19556461</ref> | + | [https://www.uniprot.org/uniprot/MMM1_ZYGRC MMM1_ZYGRC] Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jeong, H]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Lee, C]] | + | [[Category: Zygosaccharomyces rouxii CBS 732]] |
| - | [[Category: Park, J]] | + | [[Category: Jeong H]] |
| - | [[Category: Erme]] | + | [[Category: Lee C]] |
| - | [[Category: Lipid transport]] | + | [[Category: Park J]] |
| - | [[Category: Mdm12]]
| + | |
| - | [[Category: Membrane contact site]]
| + | |
| - | [[Category: Mmm1]]
| + | |
| - | [[Category: Phospholipid]]
| + | |
| Structural highlights
Function
MMM1_ZYGRC Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Publication Abstract from PubMed
The endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) comprises mitochondrial distribution and morphology 12 (Mdm12), maintenance of mitochondrial morphology 1 (Mmm1), Mdm34, and Mdm10 and mediates physical membrane contact sites and nonvesicular lipid trafficking between the ER and mitochondria in yeast. Herein, we report two crystal structures of the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain of Mmm1 and the Mdm12-Mmm1 complex at 2.8 A and 3.8 A resolution, respectively. Mmm1 adopts a dimeric SMP structure augmented with two extra structural elements at the N and C termini that are involved in tight self-association and phospholipid coordination. Mmm1 binds two phospholipids inside the hydrophobic cavity, and the phosphate ion of the distal phospholipid is specifically recognized through extensive H-bonds. A positively charged concave surface on the SMP domain not only mediates ER membrane docking but also results in preferential binding to glycerophospholipids such as phosphatidylcholine (PC), phosphatidic acid (PA), phosphatidylglycerol (PG), and phosphatidylserine (PS), some of which are substrates for lipid-modifying enzymes in mitochondria. The Mdm12-Mmm1 structure reveals two Mdm12s binding to the SMP domains of the Mmm1 dimer in a pairwise head-to-tail manner. Direct association of Mmm1 and Mdm12 generates a 210-A-long continuous hydrophobic tunnel that facilitates phospholipid transport. The Mdm12-Mmm1 complex binds all glycerophospholipids except for phosphatidylethanolamine (PE) in vitro.
Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites.,Jeong H, Park J, Jun Y, Lee C Proc Natl Acad Sci U S A. 2017 Nov 7;114(45):E9502-E9511. doi:, 10.1073/pnas.1715592114. Epub 2017 Oct 25. PMID:29078410[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jeong H, Park J, Jun Y, Lee C. Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites. Proc Natl Acad Sci U S A. 2017 Nov 7;114(45):E9502-E9511. doi:, 10.1073/pnas.1715592114. Epub 2017 Oct 25. PMID:29078410 doi:http://dx.doi.org/10.1073/pnas.1715592114
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