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| | ==Crystal structure of the human MTERF4:NSUN4:SAM ternary complex== | | ==Crystal structure of the human MTERF4:NSUN4:SAM ternary complex== |
| - | <StructureSection load='4fzv' size='340' side='right' caption='[[4fzv]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4fzv' size='340' side='right'caption='[[4fzv]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fzv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FZV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fzv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</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=4fzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzv OCA], [https://pdbe.org/4fzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzv RCSB], [https://www.ebi.ac.uk/pdbsum/4fzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NSUN4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MTERFD2, HSPC096 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzv OCA], [http://pdbe.org/4fzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fzv RCSB], [http://www.ebi.ac.uk/pdbsum/4fzv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NSUN4_HUMAN NSUN4_HUMAN]] 5-methylcytosine rRNA methyltransferase involved in mitochondrial ribosome large subunit biogenesis.<ref>PMID:21531335</ref> [[http://www.uniprot.org/uniprot/MTER2_HUMAN MTER2_HUMAN]] Regulator of mitochondrial ribosome biogenesis and translation. Binds to mitochondrial ribosomal RNAs 16S, 12S and 7S and targets NSUN4 RNA methyltransferase to the mitochondrial large ribosomal subunit (39S).<ref>PMID:21531335</ref> | + | [https://www.uniprot.org/uniprot/NSUN4_HUMAN NSUN4_HUMAN] 5-methylcytosine rRNA methyltransferase involved in mitochondrial ribosome large subunit biogenesis.<ref>PMID:21531335</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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Castano, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Choi, W S]] | + | [[Category: Castano S]] |
| - | [[Category: Garcia-Diaz, M]] | + | [[Category: Choi WS]] |
| - | [[Category: Guja, K E]] | + | [[Category: Garcia-Diaz M]] |
| - | [[Category: Hambardjieva, E]] | + | [[Category: Guja KE]] |
| - | [[Category: Mejia, E]] | + | [[Category: Hambardjieva E]] |
| - | [[Category: Yakubovskaya, E]] | + | [[Category: Mejia E]] |
| - | [[Category: Methyltransferase fold]]
| + | [[Category: Yakubovskaya E]] |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Mterf fold]]
| + | |
| - | [[Category: Rrna methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NSUN4_HUMAN 5-methylcytosine rRNA methyltransferase involved in mitochondrial ribosome large subunit biogenesis.[1]
Publication Abstract from PubMed
MTERF4 is the first MTERF family member shown to bind RNA and plays an essential role as a regulator of ribosomal biogenesis in mammalian mitochondria. It forms a complex with the rRNA methyltransferase NSUN4 and recruits it to the large ribosomal subunit. In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members. Moreover, the structure suggests a model for RNA binding by the MTERF4:NSUN4 complex, providing insight into the mechanism by which an MTERF family member facilitates rRNA methylation.
Structure of the Essential MTERF4:NSUN4 Protein Complex Reveals How an MTERF Protein Collaborates to Facilitate rRNA Modification.,Yakubovskaya E, Guja KE, Mejia E, Castano S, Hambardjieva E, Choi WS, Garcia-Diaz M Structure. 2012 Sep 25. pii: S0969-2126(12)00331-0. doi:, 10.1016/j.str.2012.08.027. PMID:23022348[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Camara Y, Asin-Cayuela J, Park CB, Metodiev MD, Shi Y, Ruzzenente B, Kukat C, Habermann B, Wibom R, Hultenby K, Franz T, Erdjument-Bromage H, Tempst P, Hallberg BM, Gustafsson CM, Larsson NG. MTERF4 regulates translation by targeting the methyltransferase NSUN4 to the mammalian mitochondrial ribosome. Cell Metab. 2011 May 4;13(5):527-39. doi: 10.1016/j.cmet.2011.04.002. PMID:21531335 doi:http://dx.doi.org/10.1016/j.cmet.2011.04.002
- ↑ Yakubovskaya E, Guja KE, Mejia E, Castano S, Hambardjieva E, Choi WS, Garcia-Diaz M. Structure of the Essential MTERF4:NSUN4 Protein Complex Reveals How an MTERF Protein Collaborates to Facilitate rRNA Modification. Structure. 2012 Sep 25. pii: S0969-2126(12)00331-0. doi:, 10.1016/j.str.2012.08.027. PMID:23022348 doi:http://dx.doi.org/10.1016/j.str.2012.08.027
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