6dcc
From Proteopedia
(Difference between revisions)
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<StructureSection load='6dcc' size='340' side='right' caption='[[6dcc]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6dcc' size='340' side='right' caption='[[6dcc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6dcc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dcc]] 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=6DCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCC 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=G5J:'>G5J</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=G5J:'>G5J</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEPCE, BCDIN3 ([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=6dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dcc OCA], [http://pdbe.org/6dcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dcc RCSB], [http://www.ebi.ac.uk/pdbsum/6dcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dcc 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=6dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dcc OCA], [http://pdbe.org/6dcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dcc RCSB], [http://www.ebi.ac.uk/pdbsum/6dcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dcc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MEPCE_HUMAN MEPCE_HUMAN]] S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it.<ref>PMID:17643375</ref> | [[http://www.uniprot.org/uniprot/MEPCE_HUMAN MEPCE_HUMAN]] S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it.<ref>PMID:17643375</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Among RNA 5'-cap structures, gamma-phosphate monomethylation is unique to a small subset of noncoding RNAs, 7SK and U6 in humans. 7SK is capped by methylphosphate capping enzyme (MePCE), which has a second nonenzymatic role as a core component of the 7SK ribonuclear protein (RNP), an essential regulator of RNA transcription. We report 2.0- and 2.1-A X-ray crystal structures of the human MePCE methyltransferase domain bound to S-adenosylhomocysteine (SAH) and uncapped or capped 7SK substrates, respectively. 7SK recognition is achieved by protein contacts to a 5'-hairpin-single-stranded RNA region, thus explaining MePCE's specificity for 7SK and U6. The structures reveal SAH and product RNA in a near-transition-state geometry. Unexpectedly, binding experiments showed that MePCE has higher affinity for capped versus uncapped 7SK, and kinetic data support a model of slow product release. This work reveals the molecular mechanism of methyl transfer and 7SK retention by MePCE for subsequent assembly of 7SK RNP. | ||
| + | |||
| + | Structural basis of 7SK RNA 5'-gamma-phosphate methylation and retention by MePCE.,Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J Nat Chem Biol. 2018 Dec 17. pii: 10.1038/s41589-018-0188-z. doi:, 10.1038/s41589-018-0188-z. PMID:30559425<ref>PMID:30559425</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6dcc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Cascio, D]] | [[Category: Cascio, D]] | ||
[[Category: Eichhorn, C]] | [[Category: Eichhorn, C]] | ||
Revision as of 06:19, 2 January 2019
Structure of methylphosphate capping enzyme methyltransferase domain in complex with 5' end of 7SK RNA
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