1zes: Difference between revisions

Revision as of 17:14, 21 February 2008

BeF3- activated PhoB receiver domain

OverviewOverview

Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.

About this StructureAbout this Structure

1ZES is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states., Bachhawat P, Swapna GV, Montelione GT, Stock AM, Structure. 2005 Sep;13(9):1353-63. PMID:16154092

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OCA

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-[[Image:1zes.gif|left|200px]]<br /><applet load="1zes" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1zes.gif|left|200px]]<br /><applet load="1zes" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1zes, resolution 1.90&Aring;" />
 '''BeF3- activated PhoB receiver domain'''<br />
 ==Overview==
-Response regulators (RRs), which undergo phosphorylation/dephosphorylation, at aspartate residues, are highly prevalent in bacterial signal, transduction. RRs typically contain an N-terminal receiver domain that, regulates the activities of a C-terminal DNA binding domain in a, phosphorylation-dependent manner. We present crystallography and solution, NMR data for the receiver domain of Escherichia coli PhoB which show, distinct 2-fold symmetric dimers in the inactive and active states. These, structures, together with the previously determined structure of the, C-terminal domain of PhoB bound to DNA, define the conformation of the, active transcription factor and provide a model for the mechanism of, activation in the OmpR/PhoB subfamily, the largest group of RRs. In the, active state, the receiver domains dimerize with 2-fold rotational, symmetry using their alpha4-beta5-alpha5 faces, while the effector domains, bind to DNA direct repeats with tandem symmetry, implying a loss of, intramolecular interactions.
+Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.
 ==About this Structure==
-ZES 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 and BEF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZES OCA].
+ZES 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> and <scene name='pdbligand=BEF:'>BEF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZES OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Bachhawat, P.]]
-[[Category: Montelione, G.T.]]
+[[Category: Montelione, G T.]]
-[[Category: Stock, A.M.]]
+[[Category: Stock, A M.]]
 [[Category: BEF]]
 [[Category: MG]]
@@ Line 24: / Line 24: @@
 [[Category: transcription factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:25:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:48 2008''