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New page: left|200px<br /><applet load="1sc5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sc5, resolution 3.26Å" /> '''Sigma-28(FliA)/FlgM ...
 
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[[Image:1sc5.gif|left|200px]]<br /><applet load="1sc5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sc5, resolution 3.26&Aring;" />
'''Sigma-28(FliA)/FlgM complex'''<br />


==Overview==
==Sigma-28(FliA)/FlgM complex==
The key regulators of bacterial transcription initiation are the sigma, factors, which direct promoter recognition and melting but only after, binding to the core RNA polymerase to form the holoenzyme. X-ray crystal, structures of the flagellar sigma, sigma(28), in complex with its, anti-sigma, FlgM, explain the inhibition mechanism of FlgM, including its, ability to attack and destabilize the sigma(28)-holoenzyme. The sigma, domains (sigma(2), sigma(3), and sigma(4)) pack together in a compact unit, with extensive interdomain interfaces that bury the promoter binding, determinants, including the -35 element recognition helix of sigma(4), which fits in an acidic groove on the surface of sigma(3). The structure, illustrates the large rearrangements that sigma(28) must undergo to form, the holoenzyme and provides insights into the regulation of sigma(28), promoter binding activity that may extend, at least in principle, to other, sigmas.
<StructureSection load='1sc5' size='340' side='right'caption='[[1sc5]], [[Resolution|resolution]] 3.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SC5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.26&#8491;</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=1sc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sc5 OCA], [https://pdbe.org/1sc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1sc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sc5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67268_AQUAE O67268_AQUAE] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity).[RuleBase:RU000715]
== 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/sc/1sc5_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=1sc5 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SC5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SC5 OCA].
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation., Sorenson MK, Ray SS, Darst SA, Mol Cell. 2004 Apr 9;14(1):127-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15068809 15068809]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Darst, S.A.]]
[[Category: Darst SA]]
[[Category: Ray, S.S.]]
[[Category: Ray SS]]
[[Category: Sorenson, M.K.]]
[[Category: Sorenson MK]]
[[Category: anti-sigma factor]]
[[Category: flagellar gene regulation]]
[[Category: rna polymerase sigma factor]]
[[Category: transcription]]
 
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