6jny: Difference between revisions
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<StructureSection load='6jny' size='340' side='right'caption='[[6jny]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='6jny' size='340' side='right'caption='[[6jny]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jny]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JNY OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6jny]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_SfI Enterobacteria phage SfI]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JNY FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.451Å</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=6jny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jny OCA], [https://pdbe.org/6jny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jny RCSB], [https://www.ebi.ac.uk/pdbsum/6jny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jny ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/M1FPN0_9CAUD M1FPN0_9CAUD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteriophage Q protein engages sigma-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for sigma-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (Q(I) and Q(II)) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, Q(I) forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well. | |||
Structural basis of Q-dependent transcription antitermination.,Shi J, Gao X, Tian T, Yu Z, Gao B, Wen A, You L, Chang S, Zhang X, Zhang Y, Feng Y Nat Commun. 2019 Jul 2;10(1):2925. doi: 10.1038/s41467-019-10958-8. PMID:31266960<ref>PMID:31266960</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6jny" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterobacteria phage SfI]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feng | [[Category: Feng Y]] | ||
[[Category: Shi | [[Category: Shi J]] | ||
Latest revision as of 10:16, 22 November 2023
Crystal structure of bacteriophage 21 Q protein
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