5zzw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA== | |
| + | <StructureSection load='5zzw' size='340' side='right'caption='[[5zzw]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zzw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZZW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=5zzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zzw OCA], [https://pdbe.org/5zzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zzw RCSB], [https://www.ebi.ac.uk/pdbsum/5zzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zzw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NDUF7_DICDI NDUF7_DICDI] Involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (PubMed:16507593, PubMed:20406883). Acts as an arginine methyltransferase and probably acts by mediating arginine methylation of ndufs2 (By similarity).[UniProtKB:Q7L592]<ref>PMID:16507593</ref> <ref>PMID:20406883</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The human protein arginine methyltransferase NDUFAF7 controls the assembly of the approximately 1-MDa mitochondrial complex I (CI; the NADH ubiquinone oxidoreductase) by methylating its subunit NDUFS2. We determined crystal structures of MidA, the Dictyostelium ortholog of NDUFAF7. The MidA catalytic core domain resembles other eukaryotic methyltransferases. However, three large core loops assemble into a regulatory domain that is likely to control ligand selection. Binding of MidA to NDUFS2 is weakened by methylation, suggesting a mechanism for methylation-controlled substrate release. Structural and bioinformatic analyses support that MidA and NDUFAF7 and their role in CI assembly are conserved from bacteria to humans, implying that protein methylation already existed in proteobacteria. In vivo studies confirmed the critical role of the MidA methyltransferase activity for CI assembly, growth, and phototaxis of Dictyostelium. Collectively, our data elucidate the origin of protein arginine methylation and its use by MidA/NDUFAF7 to regulate CI assembly. | ||
| - | + | Proteobacterial Origin of Protein Arginine Methylation and Regulation of Complex I Assembly by MidA.,Shahul Hameed UF, Sanislav O, Lay ST, Annesley SJ, Jobichen C, Fisher PR, Swaminathan K, Arold ST Cell Rep. 2018 Aug 21;24(8):1996-2004. doi: 10.1016/j.celrep.2018.07.075. PMID:30134162<ref>PMID:30134162</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5zzw" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dictyostelium discoideum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arold ST]] | ||
| + | [[Category: Hameed UFS]] | ||
| + | [[Category: Swaminathan K]] | ||
Current revision
Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA
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