7qru
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer== | |
| + | <StructureSection load='7qru' size='340' side='right'caption='[[7qru]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7qru]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalophilus_pseudofirmus Alkalihalophilus pseudofirmus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</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=7qru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qru OCA], [https://pdbe.org/7qru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qru RCSB], [https://www.ebi.ac.uk/pdbsum/7qru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qru ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1Q9PMS5_ALKPS A0A1Q9PMS5_ALKPS] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are closely related to the membrane domain of respiratory complex I. We determined the structure of the Mrp antiporter from Bacillus pseudofirmus by electron cryo-microscopy at 2.2 A resolution. The structure resolves more than 99% of the sidechains of the seven membrane subunits MrpA to MrpG plus 360 water molecules, including ~70 in putative ion translocation pathways. Molecular dynamics simulations based on the high-resolution structure revealed details of the antiport mechanism. We find that switching the position of a histidine residue between three hydrated pathways in the MrpA subunit is critical for proton transfer that drives gated trans-membrane sodium translocation. Several lines of evidence indicate that the same histidine-switch mechanism operates in respiratory complex I. | ||
| - | + | Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.,Lee Y, Haapanen O, Altmeyer A, Kuhlbrandt W, Sharma V, Zickermann V Nat Commun. 2022 Oct 14;13(1):6091. doi: 10.1038/s41467-022-33640-y. PMID:36241630<ref>PMID:36241630</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7qru" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alkalihalophilus pseudofirmus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lee Y]] | ||
Revision as of 07:17, 9 November 2022
Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer
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