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1f36

From Proteopedia

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[[Image:1f36.jpg|left|200px]]
 
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{{Structure
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==THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS==
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|PDB= 1f36 |SIZE=350|CAPTION= <scene name='initialview01'>1f36</scene>, resolution 2.65&Aring;
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<StructureSection load='1f36' size='340' side='right'caption='[[1f36]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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>
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|GENE= FIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f36 OCA], [http://www.ebi.ac.uk/pdbsum/1f36 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f36 RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f3/1f36_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''
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==See Also==
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*[[FIS protein|FIS protein]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1F36 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/9362499 9362499]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Safo, M K.]]
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[[Category: Safo MK]]
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[[Category: Yuan, H S.]]
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[[Category: Yuan HS]]
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[[Category: dna-binding protein]]
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[[Category: protein-protein interaction domain]]
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[[Category: transactivation region]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:14:52 2008''
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Current revision

THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS

PDB ID 1f36

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