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| | <StructureSection load='5gyk' size='340' side='right'caption='[[5gyk]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='5gyk' size='340' side='right'caption='[[5gyk]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gyk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GYK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gyk]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GYK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</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]] 3.596Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gyd|5gyd]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MDM12, YOL009C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5gyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gyk OCA], [https://pdbe.org/5gyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gyk RCSB], [https://www.ebi.ac.uk/pdbsum/5gyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gyk ProSAT]</span></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=5gyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gyk OCA], [http://pdbe.org/5gyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gyk RCSB], [http://www.ebi.ac.uk/pdbsum/5gyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gyk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jeong, H]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Lee, C]] | + | [[Category: Jeong H]] |
| - | [[Category: Park, J]] | + | [[Category: Lee C]] |
| - | [[Category: Ermes complex]] | + | [[Category: Park J]] |
| - | [[Category: Lipid transport]]
| + | |
| - | [[Category: Mdm12]]
| + | |
| - | [[Category: Smp domain]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
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][1] [2]
Publication Abstract from PubMed
The endoplasmic reticulum-mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the beta1-strand comprising residues 1-7. Biochemical experiments reveal a phospholipid-binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full-length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74-114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head-to-head contact, and with Mmm1 through tail-to-tail contact of SMP domains.
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex.,Jeong H, Park J, Lee C EMBO Rep. 2016 Dec;17(12):1857-1871. Epub 2016 Nov 7. PMID:27821511[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meisinger C, Pfannschmidt S, Rissler M, Milenkovic D, Becker T, Stojanovski D, Youngman MJ, Jensen RE, Chacinska A, Guiard B, Pfanner N, Wiedemann N. The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria. EMBO J. 2007 May 2;26(9):2229-39. Epub 2007 Apr 5. PMID:17410204 doi:http://dx.doi.org/10.1038/sj.emboj.7601673
- ↑ Kornmann B, Currie E, Collins SR, Schuldiner M, Nunnari J, Weissman JS, Walter P. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science. 2009 Jul 24;325(5939):477-81. Epub 2009 Jun 25. PMID:19556461 doi:http://dx.doi.org/1175088
- ↑ Jeong H, Park J, Lee C. Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex. EMBO Rep. 2016 Dec;17(12):1857-1871. Epub 2016 Nov 7. PMID:27821511 doi:http://dx.doi.org/10.15252/embr.201642706
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