5jsi: Difference between revisions
New page: '''Unreleased structure''' The entry 5jsi is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Structure of membrane protein== | |||
<StructureSection load='5jsi' size='340' side='right'caption='[[5jsi]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Actinomarina_minuta Candidatus Actinomarina minuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JSI FirstGlance]. <br> | |||
</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=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=LYR:N~6~-[(2Z,4E,6E,8E)-3,7-DIMETHYL-9-(2,6,6-TRIMETHYLCYCLOHEX-1-EN-1-YL)NONA-2,4,6,8-TETRAENYL]LYSINE'>LYR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=5jsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jsi OCA], [https://pdbe.org/5jsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jsi RCSB], [https://www.ebi.ac.uk/pdbsum/5jsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jsi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/S5DM51_9ACTN S5DM51_9ACTN] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5jsi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Candidatus Actinomarina minuta]] | |||
[[Category: Large Structures]] | |||
[[Category: Gordeliy V]] | |||
[[Category: Gushchin I]] | |||
[[Category: Kovalev K]] | |||
[[Category: Melnikov I]] | |||
[[Category: Polovinkin V]] | |||
[[Category: Popov A]] | |||
[[Category: Shevchenko V]] | |||
Latest revision as of 10:39, 8 March 2023
Structure of membrane proteinStructure of membrane protein
Structural highlights
FunctionPublication Abstract from PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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