2ly7
From Proteopedia
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==B-flap domain of RNA polymerase (B. subtilis)== | ==B-flap domain of RNA polymerase (B. subtilis)== | ||
| - | <StructureSection load='2ly7' size='340' side='right' caption='[[2ly7 | + | <StructureSection load='2ly7' size='340' side='right'caption='[[2ly7]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ly7]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ly7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LY7 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ly7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ly7 OCA], [https://pdbe.org/2ly7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ly7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ly7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ly7 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/RPOB_BACSU RPOB_BACSU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pausing during transcription elongation is a fundamental activity in all kingdoms of life. In bacteria, the essential protein NusA modulates transcriptional pausing, but its mechanism of action has remained enigmatic. By combining structural and functional studies we show that a helical rearrangement induced in NusA upon interaction with RNA polymerase is the key to its modulatory function. This conformational change leads to an allosteric re-positioning of conserved basic residues that could enable their interaction with an RNA pause hairpin that forms in the exit channel of the polymerase. This weak interaction would stabilize the paused complex and increases the duration of the transcriptional pause. Allosteric spatial re-positioning of regulatory elements may represent a general approach used across all taxa for modulation of transcription and protein-RNA interactions. | ||
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| + | RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.,Ma C, Mobli M, Yang X, Keller AN, King GF, Lewis PJ Nucleic Acids Res. 2015 Feb 17. pii: gkv108. PMID:25690895<ref>PMID:25690895</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ly7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[RNA polymerase|RNA polymerase]] | + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Mobli | + | [[Category: Mobli M]] |
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Current revision
B-flap domain of RNA polymerase (B. subtilis)
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