6uu8: Difference between revisions
New page: '''Unreleased structure''' The entry 6uu8 is ON HOLD Authors: Zuo, Y., De, S., Steitz, T.A. Description: E. coli mutant sigma-S transcription initiation complex with a 7-nt RNA (""Fres... |
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==E. coli mutant sigma-S transcription initiation complex with a 7-nt RNA ("Fresh" mutant crystal soaked with GTP, UTP, and CTP for 30 minutes)== | |||
<StructureSection load='6uu8' size='340' side='right'caption='[[6uu8]], [[Resolution|resolution]] 4.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6uu8]] is a 9 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=6UU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UU8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPO:DIPHOSPHATE'>DPO</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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=6uu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uu8 OCA], [https://pdbe.org/6uu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uu8 RCSB], [https://www.ebi.ac.uk/pdbsum/6uu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uu8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RPOC_ECOLI RPOC_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In bacteria, the dissociable sigma subunit of the RNA polymerase (RNAP) is responsible for initiating RNA synthesis from specific DNA sites. As nascent RNA grows, downstream DNA unwinds and is pulled into the RNAP, causing stress accumulation and initiation complex destabilization. Processive transcription elongation requires at least partial separation of the sigma factor from the RNAP core enzyme. Here, we present a series of transcription complexes captured between the early initiation and elongation phases via in-crystal RNA synthesis and cleavage. Crystal structures of these complexes indicate that stress accumulation during transcription initiation is not due to clashing of the growing nascent RNA with the sigma(3.2) loop, but results from scrunching of the template strand DNA that is contained inside the RNAP by the sigma(3) domain. Our results shed light on how scrunching of template-strand DNA drives both abortive initiation and sigma-RNAP core separation to transition transcription from initiation to elongation. | |||
Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation.,Zuo Y, De S, Feng Y, Steitz TA iScience. 2020 Aug 11;23(9):101445. doi: 10.1016/j.isci.2020.101445. eCollection , 2020 Sep 25. PMID:32829286<ref>PMID:32829286</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6uu8" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: De | ==See Also== | ||
*[[Sigma factor 3D structures|Sigma factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: De S]] | |||
[[Category: Steitz TA]] | |||
[[Category: Zuo Y]] | |||
Latest revision as of 13:33, 23 October 2024
E. coli mutant sigma-S transcription initiation complex with a 7-nt RNA ("Fresh" mutant crystal soaked with GTP, UTP, and CTP for 30 minutes)E. coli mutant sigma-S transcription initiation complex with a 7-nt RNA ("Fresh" mutant crystal soaked with GTP, UTP, and CTP for 30 minutes)
Structural highlights
FunctionRPOC_ECOLI DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322] Publication Abstract from PubMedIn bacteria, the dissociable sigma subunit of the RNA polymerase (RNAP) is responsible for initiating RNA synthesis from specific DNA sites. As nascent RNA grows, downstream DNA unwinds and is pulled into the RNAP, causing stress accumulation and initiation complex destabilization. Processive transcription elongation requires at least partial separation of the sigma factor from the RNAP core enzyme. Here, we present a series of transcription complexes captured between the early initiation and elongation phases via in-crystal RNA synthesis and cleavage. Crystal structures of these complexes indicate that stress accumulation during transcription initiation is not due to clashing of the growing nascent RNA with the sigma(3.2) loop, but results from scrunching of the template strand DNA that is contained inside the RNAP by the sigma(3) domain. Our results shed light on how scrunching of template-strand DNA drives both abortive initiation and sigma-RNAP core separation to transition transcription from initiation to elongation. Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation.,Zuo Y, De S, Feng Y, Steitz TA iScience. 2020 Aug 11;23(9):101445. doi: 10.1016/j.isci.2020.101445. eCollection , 2020 Sep 25. PMID:32829286[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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