1zh4

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[[Image:1zh4.gif|left|200px]]<br /><applet load="1zh4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zh4.gif|left|200px]]
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caption="1zh4, resolution 2.20&Aring;" />
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'''Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE'''<br />
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{{Structure
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|PDB= 1zh4 |SIZE=350|CAPTION= <scene name='initialview01'>1zh4</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=BEF:BERYLLIUM TRIFLUORIDE ION'>BEF</scene>
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|ACTIVITY=
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|GENE= kdpE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZH4 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=1ZH4 OCA].
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1ZH4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZH4 OCA].
==Reference==
==Reference==
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A common dimerization interface in bacterial response regulators KdpE and TorR., Toro-Roman A, Wu T, Stock AM, Protein Sci. 2005 Dec;14(12):3077-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16322582 16322582]
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A common dimerization interface in bacterial response regulators KdpE and TorR., Toro-Roman A, Wu T, Stock AM, Protein Sci. 2005 Dec;14(12):3077-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16322582 16322582]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: two-component system]]
[[Category: two-component system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:24 2008''

Revision as of 13:35, 20 March 2008


PDB ID 1zh4

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: and
Gene: kdpE (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE


Overview

Bacterial response regulators are key regulatory proteins that function as the final elements of so-called two-component signaling systems. The activities of response regulators in vivo are modulated by phosphorylation that results from interactions between the response regulator and its cognate histidine protein kinase. The level of response regulator phosphorylation, which is regulated by intra-or extracellular signals sensed by the histidine protein kinase, ultimately determines the output response that is initiated or carried out by the response regulator. We have recently hypothesized that in the OmpR/PhoB subfamily of response regulator transcription factors, this activation involves a common mechanism of dimerization using a set of highly conserved residues in the alpha4-beta5-alpha5 face. Here we report the X-ray crystal structures of the regulatory domains of response regulators TorR (1.8 A), Ca(2+)-bound KdpE (2.0 A), and Mg(2+)/BeF(3)(-)-bound KdpE (2.2 A), both members of the OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form symmetric dimers in the asymmetric unit that involve the alpha4-beta5-alpha5 face. As observed previously in other OmpR/PhoB response regulators, the dimer interfaces are mediated by highly conserved residues within this subfamily. These results provide further evidence that most all response regulators of the OmpR/ PhoB subfamily share a common mechanism of activation by dimerization.

About this Structure

1ZH4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A common dimerization interface in bacterial response regulators KdpE and TorR., Toro-Roman A, Wu T, Stock AM, Protein Sci. 2005 Dec;14(12):3077-88. PMID:16322582

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