3bqa: Difference between revisions
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'''Crystal Structure of an E.coli PhoQ Sensor Domain Mutant''' | '''Crystal Structure of an E.coli PhoQ Sensor Domain Mutant''' | ||
==Overview== | |||
The PhoP-PhoQ two-component system is a well studied bacterial signaling system that regulates virulence and stress response. Catalytic activity of the histidine kinase sensor protein PhoQ is activated by low extracellular concentrations of divalent cations such as Mg2+, and subsequently the response regulator PhoP is activated in turn through a classic phosphotransfer pathway that is typical in such systems. The PhoQ sensor domains of enteric bacteria contain an acidic cluster of residues (EDDDDAE) that has been implicated in direct binding to divalent cations. We have determined crystal structures of the wild-type Escherichia coli PhoQ periplasmic sensor domain and of a mutant variant in which the acidic cluster was neutralized to conservative uncharged residues (QNNNNAQ). The PhoQ domain structure is similar to that of DcuS and CitA sensor domains, and this PhoQ-DcuS-CitA (PDC) sensor fold is seen to be distinct from the superficially similar PAS domain fold. Analysis of the wild-type structure reveals a dimer that allows for the formation of a salt bridge across the dimer interface between Arg50' and Asp179 and with nickel ions bound to aspartate residues in the acidic cluster. The physiological importance of the salt bridge to in vivo PhoQ function has been confirmed by mutagenesis. The mutant structure has an alternative, non-physiological dimeric association. | |||
==About this Structure== | ==About this Structure== | ||
3BQA 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=3BQA OCA]. | 3BQA 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=3BQA OCA]. | ||
==Reference== | |||
Crystal structure of a functional simer of the PhoQ sensor domain., Cheung J, Bingman CA, Reyngold M, Hendrickson WA, Waldburger CD, J Biol Chem. 2008 Mar 18;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18348979 18348979] | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Histidine kinase]] | [[Category: Histidine kinase]] | ||
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[[Category: two-component regulatory system]] | [[Category: two-component regulatory system]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:32:44 2008'' | ||
Revision as of 11:32, 2 April 2008
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| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Gene: | phoQ (Escherichia coli) | ||||||
| Activity: | Histidine kinase, with EC number 2.7.13.3 | ||||||
| Domains: | PhoQ_Sensor | ||||||
| Related: | 3BQ8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of an E.coli PhoQ Sensor Domain Mutant
OverviewOverview
The PhoP-PhoQ two-component system is a well studied bacterial signaling system that regulates virulence and stress response. Catalytic activity of the histidine kinase sensor protein PhoQ is activated by low extracellular concentrations of divalent cations such as Mg2+, and subsequently the response regulator PhoP is activated in turn through a classic phosphotransfer pathway that is typical in such systems. The PhoQ sensor domains of enteric bacteria contain an acidic cluster of residues (EDDDDAE) that has been implicated in direct binding to divalent cations. We have determined crystal structures of the wild-type Escherichia coli PhoQ periplasmic sensor domain and of a mutant variant in which the acidic cluster was neutralized to conservative uncharged residues (QNNNNAQ). The PhoQ domain structure is similar to that of DcuS and CitA sensor domains, and this PhoQ-DcuS-CitA (PDC) sensor fold is seen to be distinct from the superficially similar PAS domain fold. Analysis of the wild-type structure reveals a dimer that allows for the formation of a salt bridge across the dimer interface between Arg50' and Asp179 and with nickel ions bound to aspartate residues in the acidic cluster. The physiological importance of the salt bridge to in vivo PhoQ function has been confirmed by mutagenesis. The mutant structure has an alternative, non-physiological dimeric association.
About this StructureAbout this Structure
3BQA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a functional simer of the PhoQ sensor domain., Cheung J, Bingman CA, Reyngold M, Hendrickson WA, Waldburger CD, J Biol Chem. 2008 Mar 18;. PMID:18348979
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OCA- Pages with broken file links
- Escherichia coli
- Histidine kinase
- Single protein
- Cheung, J.
- Hendrickson, W A.
- Waldburger, C D.
- Atp-binding
- Histidine kinase sensor domain
- Inner membrane
- Magnesium
- Membrane
- Metal-binding
- Nucleotide-binding
- Phosphoprotein
- Signaling protein
- Transferase
- Transmembrane
- Two-component regulatory system