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| | ==Solution structure of the delta subunit of RNA polymerase from Bacillus subtilis== | | ==Solution structure of the delta subunit of RNA polymerase from Bacillus subtilis== |
| - | <StructureSection load='2m4k' size='340' side='right'caption='[[2m4k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2m4k' size='340' side='right'caption='[[2m4k]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2m4k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M4K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2m4k]] 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=2M4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M4K FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoE, BSU37160 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | </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=2m4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4k OCA], [https://pdbe.org/2m4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m4k RCSB], [https://www.ebi.ac.uk/pdbsum/2m4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m4k 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=2m4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4k OCA], [https://pdbe.org/2m4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m4k RCSB], [https://www.ebi.ac.uk/pdbsum/2m4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m4k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RPOE_BACSU RPOE_BACSU]] Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. May function in sigma factor switching. It displaces RNA bound to RNA polymerase in a binary complex.
| + | [https://www.uniprot.org/uniprot/RPOE_BACSU RPOE_BACSU] Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. May function in sigma factor switching. It displaces RNA bound to RNA polymerase in a binary complex. |
| | <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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kaderavek, P]] | + | [[Category: Kaderavek P]] |
| - | [[Category: Krasny, L]] | + | [[Category: Krasny L]] |
| - | [[Category: Novacek, J]] | + | [[Category: Novacek J]] |
| - | [[Category: Papouskova, V]] | + | [[Category: Papouskova V]] |
| - | [[Category: Rabatinova, A]] | + | [[Category: Rabatinova A]] |
| - | [[Category: Sanderova, H]] | + | [[Category: Sanderova H]] |
| - | [[Category: Sklenar, V]] | + | [[Category: Sklenar V]] |
| - | [[Category: Zidek, L]] | + | [[Category: Zidek L]] |
| - | [[Category: Delta subunit]]
| + | |
| - | [[Category: Rna polymerase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
RPOE_BACSU Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. May function in sigma factor switching. It displaces RNA bound to RNA polymerase in a binary complex.
Publication Abstract from PubMed
The partially disordered delta subunit of RNA polymerase was studied by various NMR techniques. The structure of the well-folded N-terminal domain was determined based on inter-proton distances in NOESY spectra. The obtained structural model was compared to the previously determined structure of a truncated construct (lacking the C-terminal domain). Only marginal differences were identified, thus indicating that the first structural model was not significantly compromised by the absence of the C-terminal domain. Various (15) N relaxation experiments were employed to describe the flexibility of both domains. The relaxation data revealed that the C-terminal domain is more flexible, but its flexibility is not uniform. By using paramagnetic labels, transient contacts of the C-terminal tail with the N-terminal domain and with itself were identified. A propensity of the C-terminal domain to form beta-type structures was obtained by chemical shift analysis. Comparison with the paramagnetic relaxation enhancement indicated a well-balanced interplay of repulsive and attractive electrostatic interactions governing the conformational behavior of the C-terminal domain. The results showed that the delta subunit consists of a well-ordered N-terminal domain and a flexible C-terminal domain that exhibits a complex hierarchy of partial ordering.
Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis.,Papouskova V, Kaderavek P, Otrusinova O, Rabatinova A, Sanderova H, Novacek J, Krasny L, Sklenar V, Zidek L Chembiochem. 2013 Sep 23;14(14):1772-9. doi: 10.1002/cbic.201300226. Epub 2013, Jul 18. PMID:23868186[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Papouskova V, Kaderavek P, Otrusinova O, Rabatinova A, Sanderova H, Novacek J, Krasny L, Sklenar V, Zidek L. Structural Study of the Partially Disordered Full-Length delta Subunit of RNA Polymerase from Bacillus subtilis. Chembiochem. 2013 Sep 23;14(14):1772-9. doi: 10.1002/cbic.201300226. Epub 2013, Jul 18. PMID:23868186 doi:http://dx.doi.org/10.1002/cbic.201300226
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