1sc5

<StructureSection load='1sc5' size='340' side='right' caption='[[1sc5]], [[Resolution|resolution]] 3.26&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sc5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SC5 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rp3|1rp3]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FLIA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001]), FLGM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=1sc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sc5 OCA], [http://pdbe.org/1sc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1sc5 PDBsum]</span></td></tr>

[[http://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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1sc5_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:15068809<ref>PMID:15068809</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1sc5" style="background-color:#fffaf0;"></div>

*[[Sigma factor|Sigma factor]]

[[Category: Aquifex aeolicus huber and stetter 2001]]

[[Category: Darst, S A]]

[[Category: Ray, S S]]

[[Category: Sorenson, M K]]

[[Category: Anti-sigma factor]]

[[Category: Transcription]]