7ozo: Difference between revisions

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====
==RNA Polymerase II dimer (Class 2)==
<StructureSection load='7ozo' size='340' side='right'caption='[[7ozo]]' scene=''>
<StructureSection load='7ozo' size='340' side='right'caption='[[7ozo]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[7ozo]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa_domesticus Sus scrofa domesticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OZO FirstGlance]. <br>
</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=7ozo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ozo OCA], [https://pdbe.org/7ozo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ozo RCSB], [https://www.ebi.ac.uk/pdbsum/7ozo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ozo ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7ozo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ozo OCA], [https://pdbe.org/7ozo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ozo RCSB], [https://www.ebi.ac.uk/pdbsum/7ozo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ozo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0B8RVL1_PIG A0A0B8RVL1_PIG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic gene transcription is carried out by three RNA polymerases: Pol I, Pol II and Pol III. Although it has long been known that Pol I can form homodimers, it is unclear whether and how the two other RNA polymerases dimerize. Here we present the cryo-electron microscopy (cryo-EM) structure of a mammalian Pol II dimer at 3.5 A resolution. The structure differs from the Pol I dimer and reveals that one Pol II copy uses its RPB4-RPB7 stalk to penetrate the active centre cleft of the other copy, and vice versa, giving rise to a molecular handshake. The polymerase clamp domain is displaced and mobile, and the RPB7 oligonucleotide-binding fold mimics the DNA-RNA hybrid that occupies the cleft during active transcription. The Pol II dimer is incompatible with nucleic acid binding as required for transcription and may represent an inactive storage form of the polymerase.
Structure of an inactive RNA polymerase II dimer.,Aibara S, Dienemann C, Cramer P Nucleic Acids Res. 2021 Oct 11;49(18):10747-10755. doi: 10.1093/nar/gkab783. PMID:34530439<ref>PMID:34530439</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ozo" style="background-color:#fffaf0;"></div>
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Sus scrofa domesticus]]
[[Category: Aibara S]]
[[Category: Cramer P]]
[[Category: Dienemann C]]

Latest revision as of 15:29, 17 July 2024

RNA Polymerase II dimer (Class 2)RNA Polymerase II dimer (Class 2)

Structural highlights

7ozo is a 20 chain structure with sequence from Sus scrofa domesticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0B8RVL1_PIG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031]

Publication Abstract from PubMed

Eukaryotic gene transcription is carried out by three RNA polymerases: Pol I, Pol II and Pol III. Although it has long been known that Pol I can form homodimers, it is unclear whether and how the two other RNA polymerases dimerize. Here we present the cryo-electron microscopy (cryo-EM) structure of a mammalian Pol II dimer at 3.5 A resolution. The structure differs from the Pol I dimer and reveals that one Pol II copy uses its RPB4-RPB7 stalk to penetrate the active centre cleft of the other copy, and vice versa, giving rise to a molecular handshake. The polymerase clamp domain is displaced and mobile, and the RPB7 oligonucleotide-binding fold mimics the DNA-RNA hybrid that occupies the cleft during active transcription. The Pol II dimer is incompatible with nucleic acid binding as required for transcription and may represent an inactive storage form of the polymerase.

Structure of an inactive RNA polymerase II dimer.,Aibara S, Dienemann C, Cramer P Nucleic Acids Res. 2021 Oct 11;49(18):10747-10755. doi: 10.1093/nar/gkab783. PMID:34530439[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Aibara S, Dienemann C, Cramer P. Structure of an inactive RNA polymerase II dimer. Nucleic Acids Res. 2021 Oct 11;49(18):10747-10755. PMID:34530439 doi:10.1093/nar/gkab783

7ozo, resolution 3.80Å

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