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5JGP

Crystal structure of the nitrate/nitrite sensor NarQ fragment bound with iodide ions

Summary for 5JGP
Entry DOI10.2210/pdb5jgp/pdb
Related5IJI
DescriptorNitrate/nitrite sensor protein NarQ, NITRATE ION, IODIDE ION, ... (4 entities in total)
Functional Keywordsmembrane protein, sensor, histidine kinase, iodide, transferase, signaling protein
Biological sourceEscherichia coli (strain K12)
Cellular locationCell inner membrane ; Multi-pass membrane protein : P27896
Total number of polymer chains1
Total formula weight28397.75
Authors
Melnikov, I.,Polovinkin, V.,Popov, A.,Gordeliy, V. (deposition date: 2016-04-20, release date: 2017-05-31, Last modification date: 2025-10-01)
Primary citationMelnikov, I.,Polovinkin, V.,Kovalev, K.,Gushchin, I.,Shevtsov, M.,Shevchenko, V.,Mishin, A.,Alekseev, A.,Rodriguez-Valera, F.,Borshchevskiy, V.,Cherezov, V.,Leonard, G.A.,Gordeliy, V.,Popov, A.
Fast iodide-SAD phasing for high-throughput membrane protein structure determination.
Sci Adv, 3:e1602952-e1602952, 2017
Cited by
PubMed Abstract: 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.
PubMed: 28508075
DOI: 10.1126/sciadv.1602952
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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