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| | ==Solution structure of the N-terminal domain of NUSA from B. Subtilis== | | ==Solution structure of the N-terminal domain of NUSA from B. Subtilis== |
| - | <StructureSection load='2mt4' size='340' side='right' caption='[[2mt4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mt4' size='340' side='right'caption='[[2mt4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mt4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MT4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mt4]] 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=2MT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MT4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nusA, BSU16600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mt4 OCA], [http://pdbe.org/2mt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mt4 RCSB], [http://www.ebi.ac.uk/pdbsum/2mt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mt4 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=2mt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mt4 OCA], [https://pdbe.org/2mt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2mt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mt4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NUSA_BACSU NUSA_BACSU]] Participates in both transcription termination and antitermination.[HAMAP-Rule:MF_00945] | + | [https://www.uniprot.org/uniprot/NUSA_BACSU NUSA_BACSU] Participates in both transcription termination and antitermination.[HAMAP-Rule:MF_00945] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Lewis, P J]] | + | [[Category: Large Structures]] |
| - | [[Category: Mobli, M]] | + | [[Category: Lewis PJ]] |
| - | [[Category: Nusa]] | + | [[Category: Mobli M]] |
| - | [[Category: Rna polymerase]]
| + | |
| - | [[Category: Transcription]]
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| - | [[Category: Transcription factor]]
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| Structural highlights
Function
NUSA_BACSU Participates in both transcription termination and antitermination.[HAMAP-Rule:MF_00945]
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma C, Mobli M, Yang X, Keller AN, King GF, Lewis PJ. RNA polymerase-induced remodelling of NusA produces a pause enhancement complex. Nucleic Acids Res. 2015 Feb 17. pii: gkv108. PMID:25690895 doi:http://dx.doi.org/10.1093/nar/gkv108
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