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| ==Solution Structure of the C-terminal RpoN Domain of Sigma-54 from Aquifex aeolicus== | | ==Solution Structure of the C-terminal RpoN Domain of Sigma-54 from Aquifex aeolicus== |
- | <StructureSection load='2ahq' size='340' side='right' caption='[[2ahq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ahq' size='340' side='right'caption='[[2ahq]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2ahq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ahq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHQ FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=2ahq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahq OCA], [http://pdbe.org/2ahq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahq RCSB], [http://www.ebi.ac.uk/pdbsum/2ahq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahq 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=2ahq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahq OCA], [https://pdbe.org/2ahq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahq RCSB], [https://www.ebi.ac.uk/pdbsum/2ahq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahq ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/O66858_AQUAE O66858_AQUAE] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| ==See Also== | | ==See Also== |
- | *[[Sigma factor|Sigma factor]] | + | *[[Sigma factor 3D structures|Sigma factor 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
- | [[Category: Doucleff, M]] | + | [[Category: Large Structures]] |
- | [[Category: Malak, L T]] | + | [[Category: Doucleff M]] |
- | [[Category: Pelton, J G]] | + | [[Category: Malak LT]] |
- | [[Category: Wemmer, D E]] | + | [[Category: Pelton JG]] |
- | [[Category: Rna polymerase]] | + | [[Category: Wemmer DE]] |
- | [[Category: Sigma factor]]
| + | |
- | [[Category: Sigma-54]]
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- | [[Category: Solution structure]]
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- | [[Category: Transcription]]
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| Structural highlights
Function
O66858_AQUAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The "sigma" subunit of prokaryotic RNA polymerase allows gene-specific transcription initiation. Two sigma families have been identified, sigma70 and sigma54, which use distinct mechanisms to initiate transcription and share no detectable sequence homology. Although the sigma70-type factors have been well characterized structurally by x-ray crystallography, no high resolution structural information is available for the sigma54-type factors. Here we present the NMR-derived structure of the C-terminal domain of sigma54 from Aquifex aeolicus. This domain (Thr-323 to Gly-389), which contains the highly conserved RpoN box sequence, consists of a poorly structured N-terminal tail followed by a three-helix bundle, which is surprisingly similar to domains of the sigma70-type proteins. Residues of the RpoN box, which have previously been shown to be critical for DNA binding, form the second helix of an unpredicted helix-turn-helix motif. The homology of this structure with other DNA-binding proteins, combined with previous biochemical data, suggests how the C-terminal domain of sigma54 binds to DNA.
The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70.,Doucleff M, Malak LT, Pelton JG, Wemmer DE J Biol Chem. 2005 Dec 16;280(50):41530-6. Epub 2005 Oct 6. PMID:16210314[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doucleff M, Malak LT, Pelton JG, Wemmer DE. The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70. J Biol Chem. 2005 Dec 16;280(50):41530-6. Epub 2005 Oct 6. PMID:16210314 doi:10.1074/jbc.M509010200
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