2fbk

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[[Image:2fbk.gif|left|200px]]
 
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==The Crystal Structure of HucR from Deinococcus radiodurans==
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The line below this paragraph, containing "STRUCTURE_2fbk", creates the "Structure Box" on the page.
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<StructureSection load='2fbk' size='340' side='right'caption='[[2fbk]], [[Resolution|resolution]] 2.30&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'>[[2fbk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FBK 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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_2fbk| PDB=2fbk | SCENE= }}
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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=2fbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fbk OCA], [https://pdbe.org/2fbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fbk RCSB], [https://www.ebi.ac.uk/pdbsum/2fbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fbk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9RV71_DEIRA Q9RV71_DEIRA]
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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/fb/2fbk_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=2fbk ConSurf].
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<div style="clear:both"></div>
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'''The Crystal Structure of HucR from Deinococcus radiodurans'''
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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We report here the 2.3 A resolution structure of the hypothetical uricase regulator (HucR) from Deinococcus radiodurans R1. HucR, a member of the MarR family of DNA-binding proteins, was previously shown to repress its own expression as well as that of a uricase, a repression that is alleviated both in vivo and in vitro upon binding uric acid, the substrate for uricase. As uric acid is a potent scavenger of reactive oxygen species, and as D. radiodurans is known for its remarkable resistance to DNA-damaging agents, these observations indicate a novel oxidative stress response mechanism. The crystal structure of HucR in the absence of ligand or DNA reveals a dimer in which the DNA recognition helices are preconfigured for DNA binding. This configuration of DNA-binding domains is achieved through an apparently stable dimer interface that, in contrast to what is observed in other MarR homologs for which structures have been determined, shows little conformational heterogeneity in the absence of ligand. An additional amino-terminal segment, absent from other MarR homologs, appears to brace the principal helix of the dimerization interface. However, although HucR is preconfigured for DNA binding, the presence of a stacked pair of symmetry-related histidine residues at a central pivot point in the dimer interface suggests a mechanism for a conformational change to attenuate DNA binding.
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==About this Structure==
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2FBK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBK OCA].
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==Reference==
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The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding., Bordelon T, Wilkinson SP, Grove A, Newcomer ME, J Mol Biol. 2006 Jun 30;360(1):168-77. Epub 2006 May 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16750221 16750221]
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[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bordelon, T.]]
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[[Category: Bordelon T]]
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[[Category: Grove, A.]]
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[[Category: Grove A]]
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[[Category: Newcomer, M E.]]
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[[Category: Newcomer ME]]
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[[Category: Wilkinson, S P.]]
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[[Category: Wilkinson SP]]
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[[Category: Winged-helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:41:43 2008''
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Current revision

The Crystal Structure of HucR from Deinococcus radiodurans

PDB ID 2fbk

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