3ezi: Difference between revisions

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{{Seed}}
[[Image:3ezi.png|left|200px]]


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==Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain without Ligand==
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<StructureSection load='3ezi' size='340' side='right'caption='[[3ezi]], [[Resolution|resolution]] 1.70&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'>[[3ezi]] is a 4 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=3EZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EZI 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]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
{{STRUCTURE_3ezi|  PDB=3ezi  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ezi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ezi OCA], [https://pdbe.org/3ezi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ezi RCSB], [https://www.ebi.ac.uk/pdbsum/3ezi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ezi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NARX_ECOLI NARX_ECOLI] Acts as a sensor for nitrate/nitrite and transduces signal of nitrate availability to the NarL protein and of both nitrate/nitrite to the NarP protein. NarX probably activates NarL and NarP by phosphorylation in the presence of nitrate. NarX also plays a negative role in controlling NarL activity, probably through dephosphorylation in the absence of nitrate.
== 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/ez/3ezi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3ezi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine kinase receptors are a large family of membrane-spanning proteins found in many prokaryotes and some eukaryotes. They are a part of two-component signal transduction systems, which each comprise a sensor kinase and a response regulator and are involved with the regulation of many cellular processes. NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria. We present high-resolution X-ray crystal structures of the periplasmic sensor domain from Escherichia coli NarX in a complex with nitrate and in the apo state. Our analysis reveals that nitrate-binding induces conformation changes that result in a piston-type displacement between the N- and C-terminal helices of the periplasmic domain. Such conformational changes might represent a conserved mechanism of signaling in histidine kinases by which ligand binding is communicated across the lipid bilayer.


===Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain without Ligand===
Structural Analysis of Ligand Stimulation of the Histidine Kinase NarX.,Cheung J, Hendrickson WA Structure. 2009 Feb 13;17(2):190-201. PMID:19217390<ref>PMID:19217390</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ezi" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 19217390 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19217390}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
3EZI is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZI OCA].
[[Category: Large Structures]]
 
[[Category: Cheung J]]
==Reference==
[[Category: Hendrickson WA]]
<ref group="xtra">PMID:19217390</ref><references group="xtra"/>
[[Category: Escherichia coli k12]]
[[Category: Histidine kinase]]
[[Category: Cheung, J.]]
[[Category: Hendrickson, W A.]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Histidine kinase sensor domain]]
[[Category: Kinase]]
[[Category: Membrane]]
[[Category: Nitrate assimilation]]
[[Category: Phosphoprotein]]
[[Category: Transferase]]
[[Category: Transmembrane]]
[[Category: Two-component regulatory system]]
 
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Retrieved from "https://proteopedia.org/3ezi"