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| | <StructureSection load='3skq' size='340' side='right'caption='[[3skq]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3skq' size='340' side='right'caption='[[3skq]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3skq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SKQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3skq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SKQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MDM38, YOL027C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=3skq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3skq OCA], [https://pdbe.org/3skq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3skq RCSB], [https://www.ebi.ac.uk/pdbsum/3skq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3skq 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=3skq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3skq OCA], [https://pdbe.org/3skq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3skq RCSB], [https://www.ebi.ac.uk/pdbsum/3skq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3skq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MDM38_YEAST MDM38_YEAST]] Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266, PubMed:15138253). With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane (PubMed:20427570).<ref>PMID:11907266</ref> <ref>PMID:15138253</ref> <ref>PMID:20427570</ref>
| + | [https://www.uniprot.org/uniprot/MDM38_YEAST MDM38_YEAST] Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266, PubMed:15138253). With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane (PubMed:20427570).<ref>PMID:11907266</ref> <ref>PMID:15138253</ref> <ref>PMID:20427570</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Mitochondrial ribosomes synthesize core subunits of the inner membrane respiratory chain complexes. In mitochondria, translation is regulated by mRNA-specific activator proteins and occurs on membrane-associated ribosomes. Mdm38/Letm1 is a conserved membrane receptor for mitochondrial ribosomes and specifically involved in respiratory chain biogenesis. In addition, Mdm38 and its higher eukaryotic homolog Letm1, function as K(+) /H(+) or Ca(2+) /H(+) antiporters in the inner membrane. Here, we identify the conserved ribosome-binding domain (RBD) of Mdm38 and determine the crystal structure at 2.1 A resolution. Surprisingly, Mdm38(RBD) displays a 14-3-3-like fold despite any similarity to 14-3-3-proteins at the primary sequence level and thus represents the first 14-3-3-like protein in mitochondria. The 14-3-3-like domain is critical for respiratory chain assembly through regulation of Cox1 and Cytb translation. We show that this function can be spatially separated from the ion transport activity of the membrane integrated portion of Mdm38. On the basis of the phenotypes observed for mdm38Delta as compared to Mdm38 lacking the RBD, we suggest a model that combining ion transport and translational regulation into one molecule allows for direct coupling of ion flux across the inner membrane, and serves as a signal for the translation of mitochondrial membrane proteins via its direct association with the protein synthesis machinery.
| + | |
| - | | + | |
| - | Mdm38 is a 14-3-3-Like Receptor and Associates with the Protein Synthesis Machinery at the Inner Mitochondrial Membrane.,Lupo D, Vollmer C, Deckers M, Mick DU, Tews I, Sinning I, Rehling P Traffic. 2011 Jul 1. doi: 10.1111/j.1600-0854.2011.01239.x. PMID:21718401<ref>PMID:21718401</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3skq" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lupo, D]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Sinning, I]] | + | [[Category: Lupo D]] |
| - | [[Category: Tews, I]] | + | [[Category: Sinning I]] |
| - | [[Category: 14-3-3 like fold]] | + | [[Category: Tews I]] |
| - | [[Category: 14-3-3-like membrane protein]]
| + | |
| - | [[Category: Letm1 homolog]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Mitochondrial inner membrane]]
| + | |
| - | [[Category: Mitochondrial ribosome]]
| + | |
| - | [[Category: Respiratory chain biogenesis]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ribosome binding receptor]]
| + | |
| Structural highlights
Function
MDM38_YEAST Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation (PubMed:11907266, PubMed:15138253). With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane (PubMed:20427570).[1] [2] [3]
References
- ↑ Dimmer KS, Fritz S, Fuchs F, Messerschmitt M, Weinbach N, Neupert W, Westermann B. Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Mar;13(3):847-53. PMID:11907266 doi:10.1091/mbc.01-12-0588
- ↑ Nowikovsky K, Froschauer EM, Zsurka G, Samaj J, Reipert S, Kolisek M, Wiesenberger G, Schweyen RJ. The LETM1/YOL027 gene family encodes a factor of the mitochondrial K+ homeostasis with a potential role in the Wolf-Hirschhorn syndrome. J Biol Chem. 2004 Jul 16;279(29):30307-15. Epub 2004 May 11. PMID:15138253 doi:http://dx.doi.org/10.1074/jbc.M403607200
- ↑ Bauerschmitt H, Mick DU, Deckers M, Vollmer C, Funes S, Kehrein K, Ott M, Rehling P, Herrmann JM. Ribosome-binding proteins Mdm38 and Mba1 display overlapping functions for regulation of mitochondrial translation. Mol Biol Cell. 2010 Jun 15;21(12):1937-44. doi: 10.1091/mbc.E10-02-0101. Epub, 2010 Apr 28. PMID:20427570 doi:http://dx.doi.org/10.1091/mbc.E10-02-0101
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