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<StructureSection load='3ugo' size='340' side='right'caption='[[3ugo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3ugo' size='340' side='right'caption='[[3ugo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ugo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UGO FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ugo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UGO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.096&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ugp|3ugp]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=3ugo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugo OCA], [https://pdbe.org/3ugo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ugo RCSB], [https://www.ebi.ac.uk/pdbsum/3ugo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ugo 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=3ugo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugo OCA], [https://pdbe.org/3ugo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ugo RCSB], [https://www.ebi.ac.uk/pdbsum/3ugo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ugo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q9EZJ8_THEAQ Q9EZJ8_THEAQ]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity).[RuleBase:RU000715]
[https://www.uniprot.org/uniprot/SIGA_THEAQ SIGA_THEAQ] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.[HAMAP-Rule:MF_00963]<ref>PMID:11114902</ref> <ref>PMID:11931761</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The key step in bacterial promoter opening is recognition of the -10 promoter element (T(-12)A(-11)T(-10)A(-9)A(-8)T(-7) consensus sequence) by the RNA polymerase sigma subunit. We determined crystal structures of sigma domain 2 bound to single-stranded DNA bearing-10 element sequences. Extensive interactions occur between the protein and the DNA backbone of every -10 element nucleotide. Base-specific interactions occur primarily with A(-11) and T(-7), which are flipped out of the single-stranded DNA base stack and buried deep in protein pockets. The structures, along with biochemical data, support a model where the recognition of the -10 element sequence drives initial promoter opening as the bases of the nontemplate strand are extruded from the DNA double-helix and captured by sigma. These results provide a detailed structural basis for the critical roles of A(-11) and T(-7) in promoter melting and reveal important insights into the initiation of transcription bubble formation.
 
Structural basis for promoter-10 element recognition by the bacterial RNA polymerase sigma subunit.,Feklistov A, Darst SA Cell. 2011 Dec 9;147(6):1257-69. Epub 2011 Dec 1. PMID:22136875<ref>PMID:22136875</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ugo" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 25104]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Darst, S A]]
[[Category: Thermus aquaticus]]
[[Category: Feklistov, A]]
[[Category: Darst SA]]
[[Category: Bacterial promoter opening]]
[[Category: Feklistov A]]
[[Category: Dna binding]]
[[Category: G-quadruplex]]
[[Category: G-quartet]]
[[Category: Protein-dna complex]]
[[Category: Transcription-dna complex]]

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