3bq8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (01:38, 21 November 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3bq8.png|left|200px]]
 
-
<!--
+
==Crystal Structure of the E.coli PhoQ Sensor Domain==
-
The line below this paragraph, containing "STRUCTURE_3bq8", creates the "Structure Box" on the page.
+
<StructureSection load='3bq8' size='340' side='right'caption='[[3bq8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3bq8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQ8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-
{{STRUCTURE_3bq8| PDB=3bq8 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bq8 OCA], [https://pdbe.org/3bq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bq8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bq8 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bq8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bq8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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 Arg-50' and Asp-179 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.
-
===Crystal Structure of the E.coli PhoQ Sensor Domain===
+
Crystal structure of a functional dimer of the PhoQ sensor domain.,Cheung J, Bingman CA, Reyngold M, Hendrickson WA, Waldburger CD J Biol Chem. 2008 May 16;283(20):13762-70. Epub 2008 Mar 18. PMID:18348979<ref>PMID:18348979</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3bq8" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_18348979}}, adds the Publication Abstract to the page
+
*[[PhoP-PhoQ|PhoP-PhoQ]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 18348979 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18348979}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3BQ8 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=3BQ8 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: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Cheung J]]
-
[[Category: Cheung, J.]]
+
[[Category: Hendrickson WA]]
-
[[Category: Hendrickson, W A.]]
+
[[Category: Waldburger CD]]
-
[[Category: Waldburger, C D.]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: Histidine kinase sensor domain]]
+
-
[[Category: Inner membrane]]
+
-
[[Category: Magnesium]]
+
-
[[Category: Membrane]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Signaling protein]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Two-component regulatory system]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:49:34 2008''
+

Current revision

Crystal Structure of the E.coli PhoQ Sensor Domain

PDB ID 3bq8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bq8"
Personal tools