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| <StructureSection load='6irx' size='340' side='right'caption='[[6irx]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6irx' size='340' side='right'caption='[[6irx]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6irx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6IRX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6irx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IRX FirstGlance]. <br> |
- | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcif1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6irx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irx OCA], [http://pdbe.org/6irx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6irx RCSB], [http://www.ebi.ac.uk/pdbsum/6irx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6irx 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=6irx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irx OCA], [https://pdbe.org/6irx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6irx RCSB], [https://www.ebi.ac.uk/pdbsum/6irx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6irx ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hirano, S]] | + | [[Category: Hirano S]] |
- | [[Category: Ishitani, R]] | + | [[Category: Ishitani R]] |
- | [[Category: Nishimasu, H]] | + | [[Category: Nishimasu H]] |
- | [[Category: Nureki, O]] | + | [[Category: Nureki O]] |
- | [[Category: M6a]]
| + | |
- | [[Category: Methyltransferase]]
| + | |
- | [[Category: N6-methyladenosine]]
| + | |
- | [[Category: Rna methylation]]
| + | |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
N (6)-methyladenosine (m(6)A), a major modification of mRNAs, plays critical roles in RNA metabolism and function. In addition to the internal m(6)A, N (6), 2'-O-dimethyladenosine (m(6)Am) is present at the transcription start nucleotide of capped mRNAs in vertebrates. However, its biogenesis and functional role remain elusive. Using a reverse genetics approach, we identified PCIF1, a factor that interacts with the Ser5-phosphorylated C-terminal domain of RNA polymerase II, as cap-specific adenosine methyltransferase (CAPAM) responsible for N (6)-methylation of m(6)Am. Crystal structure of CAPAM in complex with substrates revealed the molecular basis of cap-specific m(6)A formation. A transcriptome-wide analysis revealed that N (6)-methylation of m(6)Am promotes the translation of capped mRNAs. Thus, a cap-specific m(6)A writer promotes translation of mRNAs starting from m(6)Am.
Cap-specific terminal N (6)-methylation of RNA by an RNA polymerase II-associated methyltransferase.,Akichika S, Hirano S, Shichino Y, Suzuki T, Nishimasu H, Ishitani R, Sugita A, Hirose Y, Iwasaki S, Nureki O, Suzuki T Science. 2018 Nov 22. pii: science.aav0080. doi: 10.1126/science.aav0080. PMID:30467178[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Akichika S, Hirano S, Shichino Y, Suzuki T, Nishimasu H, Ishitani R, Sugita A, Hirose Y, Iwasaki S, Nureki O, Suzuki T. Cap-specific terminal N (6)-methylation of RNA by an RNA polymerase II-associated methyltransferase. Science. 2018 Nov 22. pii: science.aav0080. doi: 10.1126/science.aav0080. PMID:30467178 doi:http://dx.doi.org/10.1126/science.aav0080
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