2pl1

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[[Image:2pl1.gif|left|200px]]<br /><applet load="2pl1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pl1.gif|left|200px]]
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caption="2pl1, resolution 1.9&Aring;" />
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'''Berrylium Fluoride activated receiver domain of E.coli PhoP'''<br />
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{{Structure
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|PDB= 2pl1 |SIZE=350|CAPTION= <scene name='initialview01'>2pl1</scene>, resolution 1.9&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <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= phoP ([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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'''Berrylium Fluoride activated receiver domain of E.coli PhoP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PL1 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=PT:'>PT</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=BEF:'>BEF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2EUB. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL1 OCA].
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2PL1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 2EUB. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PL1 OCA].
==Reference==
==Reference==
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Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride., Bachhawat P, Stock AM, J Bacteriol. 2007 Aug;189(16):5987-95. Epub 2007 Jun 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17545283 17545283]
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Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride., Bachhawat P, Stock AM, J Bacteriol. 2007 Aug;189(16):5987-95. Epub 2007 Jun 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17545283 17545283]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: virulence]]
[[Category: virulence]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:14:17 2008''

Revision as of 16:14, 20 March 2008

Image:2pl1.gif


PDB ID 2pl1

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: , and
Gene: phoP (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Berrylium Fluoride activated receiver domain of E.coli PhoP


Overview

The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg(2+). Here, we report the crystal structures of the receiver domain of Escherichia coli PhoP determined in the absence and presence of the phosphoryl analog beryllofluoride. In the presence of beryllofluoride, the active receiver domain forms a twofold symmetric dimer similar to that seen in structures of other regulatory domains from the OmpR/PhoB family, providing further evidence that members of this family utilize a common mode of dimerization in the active state. In the absence of activating agents, the PhoP receiver domain crystallizes with a similar structure, consistent with the previous observation that high concentrations can promote an active state of PhoP independent of phosphorylation.

About this Structure

2PL1 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2EUB. Full crystallographic information is available from OCA.

Reference

Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride., Bachhawat P, Stock AM, J Bacteriol. 2007 Aug;189(16):5987-95. Epub 2007 Jun 1. PMID:17545283

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