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| | ==PhoQ sensor domain (wild type): analysis of internal cavity== | | ==PhoQ sensor domain (wild type): analysis of internal cavity== |
| - | <StructureSection load='6a8u' size='340' side='right' caption='[[6a8u]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='6a8u' size='340' side='right'caption='[[6a8u]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6a8u]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6a8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A8U FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6a8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8u OCA], [http://pdbe.org/6a8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8u RCSB], [http://www.ebi.ac.uk/pdbsum/6a8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8u ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.848Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8u OCA], [https://pdbe.org/6a8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a8u RCSB], [https://www.ebi.ac.uk/pdbsum/6a8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHOQ_ECOLI PHOQ_ECOLI]] Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.<ref>PMID:10464230</ref> | + | [https://www.uniprot.org/uniprot/PHOQ_ECOLI PHOQ_ECOLI] Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.<ref>PMID:10464230</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6a8u" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6a8u" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[PhoP-PhoQ|PhoP-PhoQ]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Akiyama, Y]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Eguchi, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Ishii, E]] | + | [[Category: Akiyama Y]] |
| - | [[Category: Kato, A]] | + | [[Category: Eguchi Y]] |
| - | [[Category: Mori, H]] | + | [[Category: Ishii E]] |
| - | [[Category: Shiro, Y]] | + | [[Category: Kato A]] |
| - | [[Category: Sugimoto, H]] | + | [[Category: Mori H]] |
| - | [[Category: Taniguchi, K]] | + | [[Category: Shiro Y]] |
| - | [[Category: Utsumi, R]] | + | [[Category: Sugimoto H]] |
| - | [[Category: Yoshitani, K]] | + | [[Category: Taniguchi K]] |
| - | [[Category: Sensor protein]]
| + | [[Category: Utsumi R]] |
| - | [[Category: Signaling protein]]
| + | [[Category: Yoshitani K]] |
| Structural highlights
Function
PHOQ_ECOLI Member of the two-component regulatory system PhoP/PhoQ involved in adaptation to low Mg(2+) environments and the control of acid resistance genes. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG (By similarity). PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, or treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway; the 2 periplasmic Cys residues of MgrB are required for its action on PhoQ, which then acts on PhoP. Mediates magnesium influx to the cytosol by activation of mgtA. Promotes expression of the two-component regulatory system rstA/rstB and transcription of the hemL, mgrB, nagA, slyB, vboR and yrbL genes.[1]
Publication Abstract from PubMed
The PhoQ/PhoP two-component signal transduction system is conserved in various Gram-negative bacteria and is often involved in the expression of virulence in pathogens. The small inner membrane protein SafA activates PhoQ in Escherichia coli independently from other known signals that control PhoQ activity. We have previously shown that SafA directly interacts with the sensor domain of the periplasmic region of PhoQ (PhoQ-SD) for activation, and that a D179R mutation in PhoQ-SD attenuates PhoQ activation by SafA. In this study, structural comparison of wild-type PhoQ-SD and D179R revealed a difference in the cavity (SD (sensory domain) pocket) found in the central core of this domain. This was the only structural difference between the two proteins. Site-directed mutagenesis of the residues surrounding the SD pocket has supported the SD pocket as a site involved in PhoQ activity. Furthermore, the SD pocket has also been shown to be involved in SafA-mediated PhoQ control.
Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control.,Yoshitani K, Ishii E, Taniguchi K, Sugimoto H, Shiro Y, Akiyama Y, Kato A, Utsumi R, Eguchi Y Biosci Biotechnol Biochem. 2019 Jan 11:1-11. doi: 10.1080/09168451.2018.1562879. PMID:30632929[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kato A, Tanabe H, Utsumi R. Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: identification of extracellular Mg2+-responsive promoters. J Bacteriol. 1999 Sep;181(17):5516-20. PMID:10464230
- ↑ Yoshitani K, Ishii E, Taniguchi K, Sugimoto H, Shiro Y, Akiyama Y, Kato A, Utsumi R, Eguchi Y. Identification of an internal cavity in the PhoQ sensor domain for PhoQ activity and SafA-mediated control. Biosci Biotechnol Biochem. 2019 Jan 11:1-11. doi: 10.1080/09168451.2018.1562879. PMID:30632929 doi:http://dx.doi.org/10.1080/09168451.2018.1562879
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