2pkx
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The response regulator PhoP is part of the PhoQ/PhoP two-component system | + | 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== | ==About this Structure== | ||
| - | 2PKX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure | + | 2PKX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 2EU6. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKX OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal | + | 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] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virulence]] | [[Category: virulence]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:30 2008'' |
Revision as of 16:30, 21 February 2008
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E.coli response regulator PhoP receiver domain
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
2PKX is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2EU6. 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
Page seeded by OCA on Thu Feb 21 18:30:30 2008
