1fip

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{{Seed}}
 
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[[Image:1fip.png|left|200px]]
 
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==THE STRUCTURE OF FIS MUTANT PRO61ALA ILLUSTRATES THAT THE KINK WITHIN THE LONG ALPHA-HELIX IS NOT DUE TO THE PRESENCE OF THE PROLINE RESIDUE==
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The line below this paragraph, containing "STRUCTURE_1fip", creates the "Structure Box" on the page.
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<StructureSection load='1fip' size='340' side='right'caption='[[1fip]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1fip]] is a 4 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=1FIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FIP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#8491;</td></tr>
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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=1fip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fip OCA], [https://pdbe.org/1fip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fip RCSB], [https://www.ebi.ac.uk/pdbsum/1fip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fip ProSAT]</span></td></tr>
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{{STRUCTURE_1fip| PDB=1fip | SCENE= }}
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</table>
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== Function ==
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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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== 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/fi/1fip_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=1fip ConSurf].
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<div style="clear:both"></div>
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===THE STRUCTURE OF FIS MUTANT PRO61ALA ILLUSTRATES THAT THE KINK WITHIN THE LONG ALPHA-HELIX IS NOT DUE TO THE PRESENCE OF THE PROLINE RESIDUE===
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==See Also==
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*[[FIS protein|FIS protein]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_7961857}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 7961857 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_7961857}}
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==About this Structure==
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1FIP is a 4 chains structure of sequences 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=1FIP OCA].
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==Reference==
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<ref group="xtra">PMID:7961857</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Finkel, S E.]]
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[[Category: Large Structures]]
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[[Category: Johnson, R C.]]
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[[Category: Finkel SE]]
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[[Category: Wang, S S.]]
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[[Category: Johnson RC]]
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[[Category: Yang, W Z.]]
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[[Category: Wang SS]]
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[[Category: Yuan, H S.]]
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[[Category: Yang W-Z]]
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[[Category: Dna-binding protein]]
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[[Category: Yuan HS]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:51:30 2009''
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Current revision

THE STRUCTURE OF FIS MUTANT PRO61ALA ILLUSTRATES THAT THE KINK WITHIN THE LONG ALPHA-HELIX IS NOT DUE TO THE PRESENCE OF THE PROLINE RESIDUE

PDB ID 1fip

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