8p4a: Difference between revisions
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The | ==Structural insights into human co-transcriptional capping - structure 1== | ||
<StructureSection load='8p4a' size='340' side='right'caption='[[8p4a]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8p4a]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P4A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8p4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p4a OCA], [https://pdbe.org/8p4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p4a RCSB], [https://www.ebi.ac.uk/pdbsum/8p4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p4a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7M4DUC2_PIG A0A7M4DUC2_PIG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Co-transcriptional capping of the nascent pre-mRNA 5' end prevents degradation of RNA polymerase (Pol) II transcripts and suppresses the innate immune response. Here, we provide mechanistic insights into the three major steps of human co-transcriptional pre-mRNA capping based on six different cryoelectron microscopy (cryo-EM) structures. The human mRNA capping enzyme, RNGTT, first docks to the Pol II stalk to position its triphosphatase domain near the RNA exit site. The capping enzyme then moves onto the Pol II surface, and its guanylyltransferase receives the pre-mRNA 5'-diphosphate end. Addition of a GMP moiety can occur when the RNA is approximately 22 nt long, sufficient to reach the active site of the guanylyltransferase. For subsequent cap(1) methylation, the methyltransferase CMTR1 binds the Pol II stalk and can receive RNA after it is grown to approximately 29 nt in length. The observed rearrangements of capping factors on the Pol II surface may be triggered by the completion of catalytic reaction steps and are accommodated by domain movements in the elongation factor DRB sensitivity-inducing factor (DSIF). | |||
Structural insights into human co-transcriptional capping.,Garg G, Dienemann C, Farnung L, Schwarz J, Linden A, Urlaub H, Cramer P Mol Cell. 2023 Jun 21:S1097-2765(23)00424-0. doi: 10.1016/j.molcel.2023.06.002. PMID:37369200<ref>PMID:37369200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8p4a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Cramer P]] | |||
[[Category: Dienemann C]] | |||
[[Category: Farnung L]] | |||
[[Category: Garg G]] | |||
[[Category: Linden A]] | |||
[[Category: Schwarz J]] | |||
[[Category: Urlaub H]] | |||
Latest revision as of 11:29, 16 August 2023
Structural insights into human co-transcriptional capping - structure 1Structural insights into human co-transcriptional capping - structure 1
Structural highlights
FunctionA0A7M4DUC2_PIG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] Publication Abstract from PubMedCo-transcriptional capping of the nascent pre-mRNA 5' end prevents degradation of RNA polymerase (Pol) II transcripts and suppresses the innate immune response. Here, we provide mechanistic insights into the three major steps of human co-transcriptional pre-mRNA capping based on six different cryoelectron microscopy (cryo-EM) structures. The human mRNA capping enzyme, RNGTT, first docks to the Pol II stalk to position its triphosphatase domain near the RNA exit site. The capping enzyme then moves onto the Pol II surface, and its guanylyltransferase receives the pre-mRNA 5'-diphosphate end. Addition of a GMP moiety can occur when the RNA is approximately 22 nt long, sufficient to reach the active site of the guanylyltransferase. For subsequent cap(1) methylation, the methyltransferase CMTR1 binds the Pol II stalk and can receive RNA after it is grown to approximately 29 nt in length. The observed rearrangements of capping factors on the Pol II surface may be triggered by the completion of catalytic reaction steps and are accommodated by domain movements in the elongation factor DRB sensitivity-inducing factor (DSIF). Structural insights into human co-transcriptional capping.,Garg G, Dienemann C, Farnung L, Schwarz J, Linden A, Urlaub H, Cramer P Mol Cell. 2023 Jun 21:S1097-2765(23)00424-0. doi: 10.1016/j.molcel.2023.06.002. PMID:37369200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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