This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3cgz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:27, 12 August 2020

Crystal Structure of Salmonella Sensor Kinase PhoQ catalytic domain

Structural highlights

3cgz is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3cgy
Activity:	Histidine kinase, with EC number 2.7.13.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PHOQ_SALTY] Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. 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. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Sensor kinases in the bacterial two-component system share a unique ATP-binding Bergerat fold with the GHL (gyrase, Hsp90, and MutL) family of proteins. We demonstrated that selected GHL inhibitors bind to the catalytic domain of sensor kinase PhoQ (PhoQcat) using NMR chemical shift perturbation experiments. Using crystallographic approaches, we show that radicicol (an Hsp90 inhibitor) binds and interacts specifically with residues in the ATP-binding pocket of PhoQ. The interaction between radicicol and PhoQcat demonstrates significant similarities as well as differences compared to AMPPNP (a non-hydrolyzable ATP analog) bound to PhoQcat and radicicol bound to Hsp90. Our results suggest that GHL inhibitors may be useful lead compounds for developing sensor kinase inhibitors.

The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ.,Guarnieri MT, Zhang L, Shen J, Zhao R J Mol Biol. 2008 May 23;379(1):82-93. Epub 2008 Mar 26. PMID:18440021^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miller SI, Kukral AM, Mekalanos JJ. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc Natl Acad Sci U S A. 1989 Jul;86(13):5054-8. PMID:2544889
↑ Bearson BL, Wilson L, Foster JW. A low pH-inducible, PhoPQ-dependent acid tolerance response protects Salmonella typhimurium against inorganic acid stress. J Bacteriol. 1998 May;180(9):2409-17. PMID:9573193
↑ Sanowar S, Le Moual H. Functional reconstitution of the Salmonella typhimurium PhoQ histidine kinase sensor in proteoliposomes. Biochem J. 2005 Sep 15;390(Pt 3):769-76. PMID:15910283 doi:http://dx.doi.org/BJ20050060
↑ Guarnieri MT, Zhang L, Shen J, Zhao R. The Hsp90 inhibitor radicicol interacts with the ATP-binding pocket of bacterial sensor kinase PhoQ. J Mol Biol. 2008 May 23;379(1):82-93. Epub 2008 Mar 26. PMID:18440021 doi:10.1016/j.jmb.2008.03.036

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cgz"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Salmonella Sensor Kinase PhoQ catalytic domain==
-<StructureSection load='3cgz' size='340' side='right' caption='[[3cgz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='3cgz' size='340' side='right'caption='[[3cgz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3cgz]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CGZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3cgz]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CGZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CGZ FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cgy|3cgy]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></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=3cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cgz OCA], [http://pdbe.org/3cgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cgz RCSB], [http://www.ebi.ac.uk/pdbsum/3cgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cgz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cgz OCA], [http://pdbe.org/3cgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cgz RCSB], [http://www.ebi.ac.uk/pdbsum/3cgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cgz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Histidine kinase]]
+[[Category: Large Structures]]
 [[Category: Guarnieri, M T]]
 [[Category: Shen, J]]

3cgz

From Proteopedia

Revision as of 10:27, 12 August 2020

Crystal Structure of Salmonella Sensor Kinase PhoQ catalytic domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox