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| | ==Mdm12 from K. lactis (1-239), uniformly Lys dimethyl modified, crystallized in FOS-MEA-10== | | ==Mdm12 from K. lactis (1-239), uniformly Lys dimethyl modified, crystallized in FOS-MEA-10== |
| - | <StructureSection load='5h5c' size='340' side='right' caption='[[5h5c]], [[Resolution|resolution]] 3.31Å' scene=''> | + | <StructureSection load='5h5c' size='340' side='right'caption='[[5h5c]], [[Resolution|resolution]] 3.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h5c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H5C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h5c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H5C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h55|5h55]], [[5h54|5h54]], [[5h5a|5h5a]]</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]] 3.31Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MDM12, KLLA0C06028g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica])</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=5h5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5c OCA], [https://pdbe.org/5h5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h5c RCSB], [https://www.ebi.ac.uk/pdbsum/5h5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5c ProSAT]</span></td></tr> |
| - | <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=5h5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5c OCA], [http://pdbe.org/5h5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h5c RCSB], [http://www.ebi.ac.uk/pdbsum/5h5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MDM12_KLULA MDM12_KLULA]] 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. | + | [https://www.uniprot.org/uniprot/MDM12_KLULA MDM12_KLULA] 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. |
| | <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: Candida sphaerica]] | + | [[Category: Kluyveromyces lactis NRRL Y-1140]] |
| - | [[Category: Endo, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Kawano, S]] | + | [[Category: Endo T]] |
| - | [[Category: Quinbara, S]] | + | [[Category: Kawano S]] |
| - | [[Category: Lipid binding protein]] | + | [[Category: Quinbara S]] |
| Structural highlights
Function
MDM12_KLULA 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.
Publication Abstract from PubMed
The endoplasmic reticulum (ER)-mitochondrial encounter structure (ERMES) physically links the membranes of the ER and mitochondria in yeast. Although the ER and mitochondria cooperate to synthesize glycerophospholipids, whether ERMES directly facilitates the lipid exchange between the two organelles remains controversial. Here, we compared the x-ray structures of an ERMES subunit Mdm12 from Kluyveromyces lactis with that of Mdm12 from Saccharomyces cerevisiae and found that both Mdm12 proteins possess a hydrophobic pocket for phospholipid binding. However in vitro lipid transfer assays showed that Mdm12 alone or an Mmm1 (another ERMES subunit) fusion protein exhibited only a weak lipid transfer activity between liposomes. In contrast, Mdm12 in a complex with Mmm1 mediated efficient lipid transfer between liposomes. Mutations in Mmm1 or Mdm12 impaired the lipid transfer activities of the Mdm12-Mmm1 complex and furthermore caused defective phosphatidylserine transport from the ER to mitochondrial membranes via ERMES in vitro. Therefore, the Mmm1-Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.
Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.,Kawano S, Tamura Y, Kojima R, Bala S, Asai E, Michel AH, Kornmann B, Riezman I, Riezman H, Sakae Y, Okamoto Y, Endo T J Cell Biol. 2017 Dec 26. pii: jcb.201704119. doi: 10.1083/jcb.201704119. PMID:29279306[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kawano S, Tamura Y, Kojima R, Bala S, Asai E, Michel AH, Kornmann B, Riezman I, Riezman H, Sakae Y, Okamoto Y, Endo T. Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES. J Cell Biol. 2017 Dec 26. pii: jcb.201704119. doi: 10.1083/jcb.201704119. PMID:29279306 doi:http://dx.doi.org/10.1083/jcb.201704119
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