|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6p1c' size='340' side='right'caption='[[6p1c]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6p1c' size='340' side='right'caption='[[6p1c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p1c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_21 Bacteriophage 21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6p1c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_21 Escherichia phage 21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P1C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.005Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6p1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1c OCA], [http://pdbe.org/6p1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p1c RCSB], [http://www.ebi.ac.uk/pdbsum/6p1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1c ProSAT]</span></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=6p1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1c OCA], [https://pdbe.org/6p1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p1c RCSB], [https://www.ebi.ac.uk/pdbsum/6p1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9XJQ6_9CAUD Q9XJQ6_9CAUD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteriophage 21]] | + | [[Category: Escherichia phage 21]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ebright, R H]] | + | [[Category: Ebright RH]] |
| - | [[Category: Yin, Z]] | + | [[Category: Yin Z]] |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Q antitermination factor]]
| + | |
| - | [[Category: Q-dependent antitermination]]
| + | |
| - | [[Category: Rna polymerase]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
Q9XJQ6_9CAUD
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yin Z, Kaelber JT, Ebright RH. Structural basis of Q-dependent antitermination. 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 doi:http://dx.doi.org/10.1073/pnas.1909801116
|
