1z9c
From Proteopedia
(New page: 200px<br /><applet load="1z9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z9c, resolution 2.640Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1z9c.gif|left|200px]]<br /><applet load="1z9c" size=" | + | [[Image:1z9c.gif|left|200px]]<br /><applet load="1z9c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z9c, resolution 2.640Å" /> | caption="1z9c, resolution 2.640Å" /> | ||
'''Crystal structure of OhrR bound to the ohrA promoter: Structure of MarR family protein with operator DNA'''<br /> | '''Crystal structure of OhrR bound to the ohrA promoter: Structure of MarR family protein with operator DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mechanisms by which Bacillus subtilis OhrR, a member of the MarR | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z9C 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:// | + | 1Z9C 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9C OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brennan, R | + | [[Category: Brennan, R G.]] |
[[Category: Fuangthong, M.]] | [[Category: Fuangthong, M.]] | ||
| - | [[Category: Helmann, J | + | [[Category: Helmann, J D.]] |
[[Category: Hong, M.]] | [[Category: Hong, M.]] | ||
[[Category: bacterial transcription factor]] | [[Category: bacterial transcription factor]] | ||
| Line 22: | Line 22: | ||
[[Category: winged hth protein]] | [[Category: winged hth protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:20 2008'' |
Revision as of 14:13, 21 February 2008
|
Crystal structure of OhrR bound to the ohrA promoter: Structure of MarR family protein with operator DNA
Overview
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.
About this Structure
1Z9C is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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:16209951
Page seeded by OCA on Thu Feb 21 16:13:20 2008
