3ezi
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3ezi.jpg|left|200px]] | ||
| - | < | + | ==Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain without Ligand== |
| - | + | <StructureSection load='3ezi' size='340' side='right'caption='[[3ezi]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |
| - | -- | + | <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> |
| - | + | <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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ezi" style="background-color:#fffaf0;"></div> | |
| - | [[Category: Escherichia coli | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Cheung | + | __TOC__ |
| - | [[Category: Hendrickson | + | </StructureSection> |
| - | + | [[Category: Escherichia coli K-12]] | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Cheung J]] | |
| - | + | [[Category: Hendrickson WA]] | |
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Current revision
Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain without Ligand
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