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New page: left|200px<br /><applet load="1f36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f36, resolution 2.65Å" /> '''THE CRYSTAL STRUCTUR...
 
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[[Image:1f36.jpg|left|200px]]<br /><applet load="1f36" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f36, resolution 2.65&Aring;" />
'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS==
The Fis protein regulates site-specific DNA inversion catalyzed by a, family of DNA invertases when bound to a cis-acting recombinational, enhancer. As is often found for transactivation domains, previous crystal, structures have failed to resolve the conformation of the N-terminal, inversion activation region within the Fis dimer. A new crystal form of a, mutant Fis protein now reveals that the activation region contains two, beta-hairpin arms that protrude over 20 A from the protein core., Saturation mutagenesis identified the regulatory and structurally, important amino acids. The most critical activating residues are located, near the tips of the beta-arms. Disulfide cross-linking between the, beta-arms demonstrated that they are highly flexible in solution and that, efficient inversion activation can occur when the beta-arms are covalently, linked together. The emerging picture for this regulatory motif is that, contacts with the recombinase at the tip of the mobile beta-arms activate, the DNA invertase in the context of an invertasome complex.
<StructureSection load='1f36' size='340' side='right'caption='[[1f36]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f36]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F36 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]] 2.65&#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=1f36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f36 OCA], [https://pdbe.org/1f36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f36 RCSB], [https://www.ebi.ac.uk/pdbsum/1f36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f36 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FIS_ECOLI FIS_ECOLI] Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC.<ref>PMID:2209559</ref> <ref>PMID:8836178</ref>
== 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/f3/1f36_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=1f36 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F36 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F36 OCA].
*[[FIS protein|FIS protein]]
 
== References ==
==Reference==
<references/>
The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms., Safo MK, Yang WZ, Corselli L, Cramton SE, Yuan HS, Johnson RC, EMBO J. 1997 Nov 17;16(22):6860-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9362499 9362499]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Safo, M.K.]]
[[Category: Safo MK]]
[[Category: Yuan, H.S.]]
[[Category: Yuan HS]]
[[Category: dna-binding protein]]
[[Category: protein-protein interaction domain]]
[[Category: transactivation region]]
 
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