View source for 7q38


==Crystal structure of the mutant bacteriorhodopsin pressurized with argon==
<StructureSection load='7q38' size='340' side='right'caption='[[7q38]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q38 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AR:ARGON'>AR</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7q38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q38 OCA], [https://pdbe.org/7q38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q38 RCSB], [https://www.ebi.ac.uk/pdbsum/7q38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q38 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In this work we examine how small hydrophobic molecules such as inert gases interact with membrane proteins (MPs) at a molecular level. High pressure atmospheres of argon and krypton were used to produce noble gas derivatives of crystals of three well studied MPs (two different proton pumps and a sodium light-driven ion pump). The structures obtained using X-ray crystallography showed that the vast majority of argon and krypton binding sites were located on the outer hydrophobic surface of the MPs - a surface usually accommodating hydrophobic chains of annular lipids (which are known structural and functional determinants for MPs). In conformity with these results, supplementary in silico molecular dynamics (MD) analysis predicted even greater numbers of argon and krypton binding positions on MP surface within the bilayer. These results indicate a potential importance of such interactions, particularly as related to the phenomenon of noble gas-induced anaesthesia.

High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action.,Melnikov I, Orekhov P, Rulev M, Kovalev K, Astashkin R, Bratanov D, Ryzhykau Y, Balandin T, Bukhdruker S, Okhrimenko I, Borshchevskiy V, Bourenkov G, Mueller-Dieckmann C, van der Linden P, Carpentier P, Leonard G, Gordeliy V, Popov A Commun Biol. 2022 Apr 14;5(1):360. doi: 10.1038/s42003-022-03233-y. PMID:35422073<ref>PMID:35422073</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7q38" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Astashkin R]]
[[Category: Carpentier P]]
[[Category: Gordeliy V]]
[[Category: Kovalev K]]
[[Category: Melnikov I]]
[[Category: Popov A]]
[[Category: Rulev M]]