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6irv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the human cap-specific adenosine methyltransferase== | |
| + | <StructureSection load='6irv' size='340' side='right' caption='[[6irv]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6irv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IRV FirstGlance]. <br> | ||
| + | </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=6irv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irv OCA], [http://pdbe.org/6irv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6irv RCSB], [http://www.ebi.ac.uk/pdbsum/6irv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6irv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PCIF1_HUMAN PCIF1_HUMAN]] May play a role in transcription elongation or in coupling transcription to pre-mRNA processing through its association with the phosphorylated C-terminal domain (CTD) of RNAPII largest subunit. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:30467178</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6irv" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hirano, S]] | [[Category: Hirano, S]] | ||
| - | [[Category: Nishimasu, H]] | ||
[[Category: Ishitani, R]] | [[Category: Ishitani, R]] | ||
| + | [[Category: Nishimasu, H]] | ||
| + | [[Category: Nureki, O]] | ||
| + | [[Category: M6a]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: N6-methyladenosine]] | ||
| + | [[Category: Rna methylation]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:48, 5 December 2018
Crystal structure of the human cap-specific adenosine methyltransferase
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