8hil

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Current revision (07:38, 3 July 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8hil]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_oleracea Brassica oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HIL FirstGlance]. <br>
<table><tr><td colspan='2'>[[8hil]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_oleracea Brassica oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HIL FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.57&#8491;</td></tr>
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<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=8hil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hil OCA], [https://pdbe.org/8hil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hil RCSB], [https://www.ebi.ac.uk/pdbsum/8hil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hil 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=8hil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hil OCA], [https://pdbe.org/8hil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hil RCSB], [https://www.ebi.ac.uk/pdbsum/8hil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hil ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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In addition to the conserved RNA polymerases (Pols) I-III in eukaryotes, two atypical polymerases, Pols IV and V, specifically produce non-coding RNA in the RNA-directed DNA methylation (RdDM) pathway in plants. Here, we report on the structures of cauliflower Pol V in the free and elongation conformations. A conserved tyrosine residue of NRPE2 stacks with a dsDNA branch of the transcription bubble to potentially attenuate elongation by inducing transcription stalling. The non-template DNA strand is captured by NRPE2 to enhance backtracking, thereby increasing 3'-5' cleavage which likely underpins Pol V's high fidelity. The structures also illuminate the mechanism of Pol V transcription stalling and enhanced backtracking which may be important for Pol V's retention on chromatin to serve its function in tethering downstream factors for RdDM.
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In addition to the conserved RNA polymerases I to III (Pols I to III) in eukaryotes, two atypical polymerases, Pols IV and V, specifically produce noncoding RNA in the RNA-directed DNA methylation pathway in plants. Here, we report on the structures of cauliflower Pol V in the free and elongation conformations. A conserved tyrosine residue of NRPE2 stacks with a double-stranded DNA branch of the transcription bubble to potentially attenuate elongation by inducing transcription stalling. The nontemplate DNA strand is captured by NRPE2 to enhance backtracking, thereby increasing 3'-5' cleavage, which likely underpins Pol V's high fidelity. The structures also illuminate the mechanism of Pol V transcription stalling and enhanced backtracking, which may be important for Pol V's retention on chromatin to serve its function in tethering downstream factors for RNA-directed DNA methylation.
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Structure and mechanism of the plant RNA polymerase V.,Xie G, Du X, Hu H, Li S, Cao X, Jacobsen SE, Du J Science. 2023 Mar 9:eadf8231. doi: 10.1126/science.adf8231. PMID:36893216<ref>PMID:36893216</ref>
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Structure and mechanism of the plant RNA polymerase V.,Xie G, Du X, Hu H, Li S, Cao X, Jacobsen SE, Du J Science. 2023 Mar 24;379(6638):1209-1213. doi: 10.1126/science.adf8231. Epub 2023 , Mar 9. PMID:36893216<ref>PMID:36893216</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 8hil" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 8hil" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

A cryo-EM structure of B. oleracea RNA polymerase V at 3.57 Angstrom

PDB ID 8hil

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