8bvw

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Current revision (06:49, 24 July 2024) (edit) (undo)
 
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<StructureSection load='8bvw' size='340' side='right'caption='[[8bvw]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='8bvw' size='340' side='right'caption='[[8bvw]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[8bvw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [https://en.wikipedia.org/wiki/Unidentified_adenovirus Unidentified adenovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BVW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[8bvw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BVW 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=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 4&#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=SF4:IRON/SULFUR+CLUSTER'>SF4</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=8bvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bvw OCA], [https://pdbe.org/8bvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bvw RCSB], [https://www.ebi.ac.uk/pdbsum/8bvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bvw 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=8bvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bvw OCA], [https://pdbe.org/8bvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bvw RCSB], [https://www.ebi.ac.uk/pdbsum/8bvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bvw ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/ERCC3_HUMAN ERCC3_HUMAN] ATP-dependent 3'-5' DNA helicase, component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage.<ref>PMID:10024882</ref>
[https://www.uniprot.org/uniprot/ERCC3_HUMAN ERCC3_HUMAN] ATP-dependent 3'-5' DNA helicase, component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Acts by opening DNA either around the RNA transcription start site or the DNA damage.<ref>PMID:10024882</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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At active human genes, the +1 nucleosome is located downstream of the RNA polymerase II (RNA Pol II) pre-initiation complex (PIC). However, at inactive genes, the +1 nucleosome is found further upstream, at a promoter-proximal location. Here, we establish a model system to show that a promoter-proximal +1 nucleosome can reduce RNA synthesis in vivo and in vitro, and we analyze its structural basis. We find that the PIC assembles normally when the edge of the +1 nucleosome is located 18 base pairs (bp) downstream of the transcription start site (TSS). However, when the nucleosome edge is located further upstream, only 10 bp downstream of the TSS, the PIC adopts an inhibited state. The transcription factor IIH (TFIIH) shows a closed conformation and its subunit XPB contacts DNA with only one of its two ATPase lobes, inconsistent with DNA opening. These results provide a mechanism for nucleosome-dependent regulation of transcription initiation.
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Structural basis of transcription reduction by a promoter-proximal +1 nucleosome.,Abril-Garrido J, Dienemann C, Grabbe F, Velychko T, Lidschreiber M, Wang H, Cramer P Mol Cell. 2023 Jun 1;83(11):1798-1809.e7. doi: 10.1016/j.molcel.2023.04.011. Epub , 2023 May 5. PMID:37148879<ref>PMID:37148879</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8bvw" 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/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sus scrofa]]
 
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[[Category: Unidentified adenovirus]]
 
[[Category: Abril-Garrido J]]
[[Category: Abril-Garrido J]]
[[Category: Cramer P]]
[[Category: Cramer P]]

Current revision

RNA polymerase II pre-initiation complex with the distal +1 nucleosome (PIC-Nuc18W)

PDB ID 8bvw

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