1xhf
From Proteopedia
(New page: 200px<br /><applet load="1xhf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xhf, resolution 2.152Å" /> '''Crystal structure o...) |
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| - | [[Image:1xhf.gif|left|200px]]<br /><applet load="1xhf" size=" | + | [[Image:1xhf.gif|left|200px]]<br /><applet load="1xhf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xhf, resolution 2.152Å" /> | caption="1xhf, resolution 2.152Å" /> | ||
'''Crystal structure of the bef3-activated receiver domain of redox response regulator arca'''<br /> | '''Crystal structure of the bef3-activated receiver domain of redox response regulator arca'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Escherichia coli react to changes from aerobic to anaerobic conditions of | + | Escherichia coli react to changes from aerobic to anaerobic conditions of growth using the ArcA-ArcB two-component signal transduction system. This system, in conjunction with other proteins, regulates the respiratory metabolic pathways in the organism. ArcA is a member of the OmpR/PhoB subfamily of response regulator transcription factors that are known to regulate transcription by binding in tandem to target DNA direct repeats. It is still unclear in this subfamily how activation by phosphorylation of the regulatory domain of response regulators stimulates DNA binding by the effector domain and how dimerization and domain orientation, as well as intra- and intermolecular interactions, affect this process. In order to address these questions we have solved the crystal structures of the regulatory domain of ArcA in the presence and absence of the phosphoryl analog, BeF3-. In the crystal structures, the regulatory domain of ArcA forms a symmetric dimer mediated by the alpha4-beta5-alpha5 face of the protein and involving a number of residues that are highly conserved in the OmpR/PhoB subfamily. It is hypothesized that members of this subfamily use a common mechanism of regulation by dimerization. Additional biophysical studies were employed to probe the oligomerization state of ArcA, as well as its individual domains, in solution. The solution studies show the propensity of the individual domains to associate into oligomers larger than the dimer observed for the intact protein, and suggest that the C-terminal DNA-binding domain also plays a role in oligomerization. |
==About this Structure== | ==About this Structure== | ||
| - | 1XHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, BEF, BF4 and BF2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=BEF:'>BEF</scene>, <scene name='pdbligand=BF4:'>BF4</scene> and <scene name='pdbligand=BF2:'>BF2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XHF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Mack, T | + | [[Category: Mack, T R.]] |
| - | [[Category: Stock, A | + | [[Category: Stock, A M.]] |
[[Category: Toro-Roman, A.]] | [[Category: Toro-Roman, A.]] | ||
[[Category: BEF]] | [[Category: BEF]] | ||
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[[Category: two-component system; gene regulation; transcription factor; anoxic redox control; doubly wound five-stranded beta/alpha fold]] | [[Category: two-component system; gene regulation; transcription factor; anoxic redox control; doubly wound five-stranded beta/alpha fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:48 2008'' |
Revision as of 13:54, 21 February 2008
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Crystal structure of the bef3-activated receiver domain of redox response regulator arca
Overview
Escherichia coli react to changes from aerobic to anaerobic conditions of growth using the ArcA-ArcB two-component signal transduction system. This system, in conjunction with other proteins, regulates the respiratory metabolic pathways in the organism. ArcA is a member of the OmpR/PhoB subfamily of response regulator transcription factors that are known to regulate transcription by binding in tandem to target DNA direct repeats. It is still unclear in this subfamily how activation by phosphorylation of the regulatory domain of response regulators stimulates DNA binding by the effector domain and how dimerization and domain orientation, as well as intra- and intermolecular interactions, affect this process. In order to address these questions we have solved the crystal structures of the regulatory domain of ArcA in the presence and absence of the phosphoryl analog, BeF3-. In the crystal structures, the regulatory domain of ArcA forms a symmetric dimer mediated by the alpha4-beta5-alpha5 face of the protein and involving a number of residues that are highly conserved in the OmpR/PhoB subfamily. It is hypothesized that members of this subfamily use a common mechanism of regulation by dimerization. Additional biophysical studies were employed to probe the oligomerization state of ArcA, as well as its individual domains, in solution. The solution studies show the propensity of the individual domains to associate into oligomers larger than the dimer observed for the intact protein, and suggest that the C-terminal DNA-binding domain also plays a role in oligomerization.
About this Structure
1XHF is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face., Toro-Roman A, Mack TR, Stock AM, J Mol Biol. 2005 May 27;349(1):11-26. Epub 2005 Apr 7. PMID:15876365
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