5zu0
From Proteopedia
(Difference between revisions)
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==Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA== | ==Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA== | ||
| - | <StructureSection load='5zu0' size='340' side='right' caption='[[5zu0]], [[Resolution|resolution]] 2.76Å' scene=''> | + | <StructureSection load='5zu0' size='340' side='right'caption='[[5zu0]], [[Resolution|resolution]] 2.76Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zu0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[5zu0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZU0 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ztz|5ztz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ztz|5ztz]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">midA, DDB_G0282615 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">midA, DDB_G0282615 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_II_protein_arginine_methyltransferase Type II protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.320 2.1.1.320] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_II_protein_arginine_methyltransferase Type II protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.320 2.1.1.320] </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=5zu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zu0 OCA], [http://pdbe.org/5zu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zu0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zu0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zu0 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=5zu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zu0 OCA], [http://pdbe.org/5zu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zu0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zu0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zu0 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://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> | [[http://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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zu0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Dicdi]] |
| + | [[Category: Large Structures]] | ||
[[Category: Type II protein arginine methyltransferase]] | [[Category: Type II protein arginine methyltransferase]] | ||
[[Category: Arold, S T]] | [[Category: Arold, S T]] | ||
Revision as of 12:44, 25 December 2019
Proteobacterial origin of protein arginine methylation and regulation of Complex I assembly by MidA
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