1z91

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[[Image:1z91.gif|left|200px]]
 
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{{Structure
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==x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein==
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|PDB= 1z91 |SIZE=350|CAPTION= <scene name='initialview01'>1z91</scene>, resolution 2.50&Aring;
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<StructureSection load='1z91' size='340' side='right'caption='[[1z91]], [[Resolution|resolution]] 2.50&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'>[[1z91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z91 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]] 2.5&#8491;</td></tr>
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|GENE= ohrR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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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=1z91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z91 OCA], [https://pdbe.org/1z91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z91 RCSB], [https://www.ebi.ac.uk/pdbsum/1z91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z91 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=1z91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z91 OCA], [http://www.ebi.ac.uk/pdbsum/1z91 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z91 RCSB]</span>
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[https://www.uniprot.org/uniprot/OHRR_BACSU OHRR_BACSU] Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.<ref>PMID:11418552</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/z9/1z91_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=1z91 ConSurf].
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<div style="clear:both"></div>
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'''x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein'''
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==See Also==
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*[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]]
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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==Overview==
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== References ==
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The mechanisms by which Bacillus subtilis OhrR, a member of the MarR family of transcription regulators, binds the ohrA operator and is induced by oxidation of its lone cysteine residue by organic hydroperoxides to sulphenic acid are unknown. Here, we describe the crystal structures of reduced OhrR and an OhrR-ohrA operator complex. To bind DNA, OhrR employs a chimeric winged helix-turn-helix DNA binding motif, which is composed of extended eukaryotic-like wings, prokaryotic helix-turn-helix motifs, and helix-helix elements. The reactivity of the peroxide-sensing cysteine is not modulated by proximal basic residues but largely by the positive dipole of helix alpha1. Induction originates from the alleviation of intersubunit steric clash between the sulphenic acid moieties of the oxidized sensor cysteines and nearby tyrosines and methionines. The structure of the OhrR-ohrA operator complex reveals the DNA binding mechanism of the entire MarR family and suggests a common inducer binding pocket.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1Z91 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z91 OCA].
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==Reference==
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Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family., Hong M, Fuangthong M, Helmann JD, Brennan RG, Mol Cell. 2005 Oct 7;20(1):131-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16209951 16209951]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brennan, R G.]]
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[[Category: Brennan RG]]
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[[Category: Fuangthong, M.]]
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[[Category: Fuangthong M]]
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[[Category: Helmann, J D.]]
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[[Category: Helmann JD]]
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[[Category: Hong, M.]]
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[[Category: Hong M]]
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[[Category: bacterial transcription factor]]
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[[Category: marr family]]
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[[Category: ohrr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:32:21 2008''
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Current revision

x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein

PDB ID 1z91

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