View source for 1jkq


==Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations==
<StructureSection load='1jkq' size='340' side='right' caption='[[1jkq]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jkq]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JKQ FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hcr|1hcr]], [[1ijw|1ijw]], [[1jj6|1jj6]], [[1jj8|1jj8]], [[1jko|1jko]], [[1jkp|1jkp]], [[1jkr|1jkr]]</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=1jkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jkq OCA], [http://pdbe.org/1jkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jkq RCSB], [http://www.ebi.ac.uk/pdbsum/1jkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jkq ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/HIN_SALTY HIN_SALTY]] A DNA fragment of approximately 900 base pairs, adjacent to the fljB (H2) gene, which specifies the synthesis of phase-2 flagellin, can exist in either orientation with respect to fljB. The orientation of the inversion region controls expression of fljB. The hin gene occupies about two-thirds of the inversion region; it is required for the inversion of the fljB controlling region. 
== 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/jk/1jkq_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=1jkq ConSurf].
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== Publication Abstract from PubMed ==
The Hin recombinase specifically recognizes its DNA-binding site by means of both major and minor groove interactions. A previous X-ray structure, together with new structures of the Hin DNA-binding domain bound to a recombination half-site that were solved as part of the present study, have revealed that two ordered water molecules are present within the major groove interface. In this report, we test the importance of these waters directly by X-ray crystal structure analysis of complexes with four mutant DNA sequences. These structures, combined with their Hin-binding properties, provide strong support for the critical importance of one of the intermediate waters. A lesser but demonstrable role is ascribed to the second water molecule. The mutant structures also illustrate the prominent roles of thymine methyls both in stabilizing intermediate waters and in interfering with water or amino acid side chain interactions with DNA.

Testing water-mediated DNA recognition by the Hin recombinase.,Chiu TK, Sohn C, Dickerson RE, Johnson RC EMBO J. 2002 Feb 15;21(4):801-14. PMID:11847127<ref>PMID:11847127</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 1jkq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chiu, T K]]
[[Category: Dickerson, R E]]
[[Category: Johnson, R C]]
[[Category: Sohn, C]]
[[Category: Dna binding protein-dna complex]]
[[Category: G9t mutant]]
[[Category: Hin recombinase]]
[[Category: Protein-dna complex]]
[[Category: Water-mediated recognition]]