1z91: Difference between revisions

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New page: left|200px<br /><applet load="1z91" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z91, resolution 2.50Å" /> '''x-ray crystal struct...
 
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[[Image:1z91.gif|left|200px]]<br /><applet load="1z91" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1z91, resolution 2.50&Aring;" />
'''x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein'''<br />


==Overview==
==x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein==
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.
<StructureSection load='1z91' size='340' side='right'caption='[[1z91]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>
== 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/z9/1z91_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=1z91 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1Z91 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z91 OCA].
*[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]]
 
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
==Reference==
== References ==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16209951 16209951]
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brennan, R.G.]]
[[Category: Brennan RG]]
[[Category: Fuangthong, M.]]
[[Category: Fuangthong M]]
[[Category: Helmann, J.D.]]
[[Category: Helmann JD]]
[[Category: Hong, M.]]
[[Category: Hong M]]
[[Category: bacterial transcription factor]]
[[Category: marr family]]
[[Category: ohrr]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:18:43 2007''

Latest revision as of 12:02, 14 February 2024

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

Structural highlights

1z91 is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OHRR_BACSU Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Fuangthong M, Atichartpongkul S, Mongkolsuk S, Helmann JD. OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J Bacteriol. 2001 Jul;183(14):4134-41. PMID:11418552 doi:http://dx.doi.org/10.1128/JB.183.14.4134-4141.2001

1z91, resolution 2.50Å

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