View source for 5jgp


==Crystal structure of the nitrate/nitrite sensor NarQ fragment bound with iodide ions==
<StructureSection load='5jgp' size='340' side='right'caption='[[5jgp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jgp]] is a 1 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=5JGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JGP 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=5jgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jgp OCA], [https://pdbe.org/5jgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jgp RCSB], [https://www.ebi.ac.uk/pdbsum/5jgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jgp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NARQ_ECOLI NARQ_ECOLI] Acts as a sensor for nitrate/nitrite and transduces signal of nitrate/nitrite availability to the NarL/NarP proteins. NarQ probably activates NarL and NarP by phosphorylation. NarQ probably negatively regulates the NarL protein by dephosphorylation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane proteins via iodide-single-wavelength anomalous diffraction (I-SAD). The potential universality of the method is based on a common feature of membrane proteins-the availability at the hydrophobic-hydrophilic interface of positively charged amino acid residues with which iodide strongly interacts. We demonstrate the solution using I-SAD of four crystal structures representing different classes of membrane proteins, including a human G protein-coupled receptor (GPCR), and we show that I-SAD can be applied using data collection strategies based on either standard or serial x-ray crystallography techniques.

Fast iodide-SAD phasing for high-throughput membrane protein structure determination.,Melnikov I, Polovinkin V, Kovalev K, Gushchin I, Shevtsov M, Shevchenko V, Mishin A, Alekseev A, Rodriguez-Valera F, Borshchevskiy V, Cherezov V, Leonard GA, Gordeliy V, Popov A Sci Adv. 2017 May 12;3(5):e1602952. doi: 10.1126/sciadv.1602952. eCollection 2017, May. PMID:28508075<ref>PMID:28508075</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jgp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Gordeliy V]]
[[Category: Melnikov I]]
[[Category: Polovinkin V]]
[[Category: Popov A]]