View source for 7qru


==Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer==
<StructureSection load='7qru' size='340' side='right'caption='[[7qru]], [[Resolution|resolution]] 2.24&Aring;' 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.24&#8491;</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/MRPC_ALKPO MRPC_ALKPO] Mnh complex is a Na(+)Li(+)/H(+) antiporter involved in Na(+) and/or Li(+) excretion and Na(+) resistance. Na(+)/H(+) antiport consumes a transmembrane electrical potential, and is thus inferred to be electrogenic. Does not transport K(+), Ca(2+) or Mg(2+).
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qru" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Alkalihalophilus pseudofirmus]]
[[Category: Large Structures]]
[[Category: Lee Y]]