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[[Image:2ahq.gif|left|200px]]
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{{STRUCTURE_2ahq|  PDB=2ahq  |  SCENE=  }}
'''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]]' scene=''>
== Structural highlights ==
<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='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=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>
== Function ==
[https://www.uniprot.org/uniprot/O66858_AQUAE O66858_AQUAE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/2ahq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ahq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:16210314</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2AHQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHQ OCA].
</div>
<div class="pdbe-citations 2ahq" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16210314 16210314]
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Doucleff, M.]]
[[Category: Doucleff M]]
[[Category: Malak, L T.]]
[[Category: Malak LT]]
[[Category: Pelton, J G.]]
[[Category: Pelton JG]]
[[Category: Wemmer, D E.]]
[[Category: Wemmer DE]]
[[Category: Rna polymerase]]
[[Category: Sigma-54,sigma factor]]
[[Category: Solution structure]]
[[Category: Transcription]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:03:48 2008''
Retrieved from "https://proteopedia.org/2ahq"