6p1a: Difference between revisions

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'''Unreleased structure'''


The entry 6p1a is ON HOLD
==Transcription antitermination factor Q21 in complex with Q21-binding-element DNA==
<StructureSection load='6p1a' size='340' side='right'caption='[[6p1a]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6p1a]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Phage_21 Phage 21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P1A 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]] 2.837&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6p1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1a OCA], [https://pdbe.org/6p1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p1a RCSB], [https://www.ebi.ac.uk/pdbsum/6p1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9XJQ6_9CAUD Q9XJQ6_9CAUD]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lambdoid bacteriophage Q protein mediates the switch from middle to late bacteriophage gene expression by enabling RNA polymerase (RNAP) to read through transcription terminators preceding bacteriophage late genes. Q loads onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element (SDPE) to yield a Q-loading complex, and Q subsequently translocates with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. Here, we report high-resolution structures of 4 states on the pathway of antitermination by Q from bacteriophage 21 (Q21): Q21, the Q21-QBE complex, the Q21-loading complex, and the Q21-loaded complex. The results show that Q21 forms a torus, a "nozzle," that narrows and extends the RNAP RNA-exit channel, extruding topologically linked single-stranded RNA and preventing the formation of pause and terminator hairpins.


Authors: Yin, Z., Ebright, R.H.
Structural basis of Q-dependent antitermination.,Yin Z, Kaelber JT, Ebright RH Proc Natl Acad Sci U S A. 2019 Sep 10;116(37):18384-18390. doi:, 10.1073/pnas.1909801116. Epub 2019 Aug 27. PMID:31455742<ref>PMID:31455742</ref>


Description: Transcription antitermination factor Q21 in complex with Q21-binding-elment DNA
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Ebright, R.H]]
<div class="pdbe-citations 6p1a" style="background-color:#fffaf0;"></div>
[[Category: Yin, Z]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phage 21]]
[[Category: Ebright RH]]
[[Category: Yin Z]]

Latest revision as of 07:21, 11 October 2023

Transcription antitermination factor Q21 in complex with Q21-binding-element DNA

6p1a, resolution 2.84Å

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