View source for 4pxk


==Crystal structure of Haloarcula marismortui bacteriorhodopsin I D94N mutant==
<StructureSection load='4pxk' size='340' side='right'caption='[[4pxk]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pxk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui_ATCC_43049 Haloarcula marismortui ATCC 43049]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PXK 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFA:EICOSANE'>LFA</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=4pxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pxk OCA], [https://pdbe.org/4pxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pxk RCSB], [https://www.ebi.ac.uk/pdbsum/4pxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pxk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACR1_HALMA BACR1_HALMA] Light-driven proton pump.<ref>PMID:20802037</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mutant, at the resolution of 2.5 A. While the HmBRI retinal-binding pocket and proton donor site are similar to those of other archaeal proton pumps, its proton release region is extended and contains additional water molecules. The protein's fold is reinforced by three novel inter-helical hydrogen bonds, two of which result from double substitutions relative to Halobacterium salinarum bacteriorhodopsin and other similar proteins. Despite the expression in Escherichia coli and consequent absence of native lipids, the protein assembles as a trimer in crystals. The unique extended loop between the helices D and E of HmBRI makes contacts with the adjacent protomer and appears to stabilize the interface. Many lipidic hydrophobic tail groups are discernible in the membrane region, and their positions are similar to those of archaeal isoprenoid lipids in the crystals of other proton pumps, isolated from native or native-like sources. All these features might explain the HmBRI properties and establish the protein as a novel model for the microbial rhodopsin proton pumping studies.

Crystal Structure of Escherichia coli-Expressed Haloarcula marismortui Bacteriorhodopsin I in the Trimeric Form.,Shevchenko V, Gushchin I, Polovinkin V, Round E, Borshchevskiy V, Utrobin P, Popov A, Balandin T, Buldt G, Gordeliy V PLoS One. 2014 Dec 5;9(12):e112873. doi: 10.1371/journal.pone.0112873., eCollection 2014. PMID:25479443<ref>PMID:25479443</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pxk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haloarcula marismortui ATCC 43049]]
[[Category: Large Structures]]
[[Category: Gordeliy V]]
[[Category: Gushchin I]]
[[Category: Polovinkin V]]
[[Category: Shevchenko V]]