6z9t
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Transcription termination intermediate complex 5== |
| - | <StructureSection load='6z9t' size='340' side='right'caption='[[6z9t]]' scene=''> | + | <StructureSection load='6z9t' size='340' side='right'caption='[[6z9t]], [[Resolution|resolution]] 4.10Å' 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'>[[6z9t]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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=6Z9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z9T 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=6z9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z9t OCA], [https://pdbe.org/6z9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z9t RCSB], [https://www.ebi.ac.uk/pdbsum/6z9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z9t 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]] 4.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <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=6z9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z9t OCA], [https://pdbe.org/6z9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z9t RCSB], [https://www.ebi.ac.uk/pdbsum/6z9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z9t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NUSA_ECOLI NUSA_ECOLI] Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.<ref>PMID:6263495</ref> <ref>PMID:6265785</ref> <ref>PMID:6199039</ref> <ref>PMID:2821282</ref> <ref>PMID:7536848</ref> <ref>PMID:9139668</ref> <ref>PMID:11719185</ref> <ref>PMID:20696893</ref> <ref>PMID:21922055</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) rho on a pathway to terminating NusA/NusG-modified elongation complexes. An open rho ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the rho ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping rho subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that rho, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state. | ||
| + | |||
| + | Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho.,Said N, Hilal T, Sunday ND, Khatri A, Burger J, Mielke T, Belogurov GA, Loll B, Sen R, Artsimovitch I, Wahl MC Science. 2021 Jan 1;371(6524):eabd1673. doi: 10.1126/science.abd1673. Epub 2020 , Nov 26. PMID:33243850<ref>PMID:33243850</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6z9t" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Helicase 3D structures|Helicase 3D structures]] | ||
| + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Synthetic construct]] |
| + | [[Category: Hilal T]] | ||
| + | [[Category: Loll B]] | ||
| + | [[Category: Said N]] | ||
| + | [[Category: Wahl MC]] | ||
Current revision
Transcription termination intermediate complex 5
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