7qv9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM structure of bacterial transcription intermediate complex mediated by activator PspF== | |
| + | <StructureSection load='7qv9' size='340' side='right'caption='[[7qv9]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7qv9]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QV9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=AF3:ALUMINUM+FLUORIDE'>AF3</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=7qv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qv9 OCA], [https://pdbe.org/7qv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qv9 RCSB], [https://www.ebi.ac.uk/pdbsum/7qv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qv9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RPOA_ECOLI RPOA_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gene transcription is carried out by RNA polymerase (RNAP) and requires the conversion of the initial closed promoter complex, where DNA is double stranded, to a transcription-competent open promoter complex, where DNA is opened up. In bacteria, RNAP relies on sigma factors for its promoter specificities. Using a special form of sigma factor (sigma(54)), which forms a stable closed complex and requires its activator that belongs to the AAA+ ATPases (ATPases associated with diverse cellular activities), we obtained cryo-electron microscopy structures of transcription initiation complexes that reveal a previously unidentified process of DNA melting opening. The sigma(54) amino terminus threads through the locally opened up DNA and then becomes enclosed by the AAA+ hexameric ring in the activator-bound intermediate complex. Our structures suggest how ATP hydrolysis by the AAA+ activator could remove the sigma(54) inhibition while helping to open up DNA, using sigma(54) amino-terminal peptide as a pry bar. | ||
| - | + | Mechanisms of DNA opening revealed in AAA+ transcription complex structures.,Ye F, Gao F, Liu X, Buck M, Zhang X Sci Adv. 2022 Dec 21;8(51):eadd3479. doi: 10.1126/sciadv.add3479. Epub 2022 Dec , 21. PMID:36542713<ref>PMID:36542713</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7qv9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Klebsiella pneumoniae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ye FZ]] | ||
| + | [[Category: Zhang XD]] | ||
Current revision
CryoEM structure of bacterial transcription intermediate complex mediated by activator PspF
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