7p1k

==Cryo EM structure of bison NHA2 in nano disc structure==

<table><tr><td colspan='2'>[[7p1k]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P1K FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=T7X:PHOSPHATIDYLINOSITOL'>T7X</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr>

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== Publication Abstract from PubMed ==

The Na(+)/H(+) exchanger SLC9B2, also known as NHA2, correlates with the long-sought-after Na(+)/Li(+) exchanger linked to the pathogenesis of diabetes mellitus and essential hypertension in humans. Despite the functional importance of NHA2, structural information and the molecular basis for its ion-exchange mechanism have been lacking. Here we report the cryo-EM structures of bison NHA2 in detergent and in nanodiscs, at 3.0 and 3.5 A resolution, respectively. The bison NHA2 structure, together with solid-state membrane-based electrophysiology, establishes the molecular basis for electroneutral ion exchange. NHA2 consists of 14 transmembrane (TM) segments, rather than the 13 TMs previously observed in mammalian Na(+)/H(+) exchangers (NHEs) and related bacterial antiporters. The additional N-terminal helix in NHA2 forms a unique homodimer interface with a large intracellular gap between the protomers, which closes in the presence of phosphoinositol lipids. We propose that the additional N-terminal helix has evolved as a lipid-mediated remodeling switch for the regulation of NHA2 activity.

Structure, mechanism and lipid-mediated remodeling of the mammalian Na(+)/H(+) exchanger NHA2.,Matsuoka R, Fudim R, Jung S, Zhang C, Bazzone A, Chatzikyriakidou Y, Robinson CV, Nomura N, Iwata S, Landreh M, Orellana L, Beckstein O, Drew D Nat Struct Mol Biol. 2022 Feb;29(2):108-120. doi: 10.1038/s41594-022-00738-2., Epub 2022 Feb 16. PMID:35173351<ref>PMID:35173351</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Drew, D]]

[[Category: Fudim, R]]

[[Category: Jung, S]]

[[Category: Matsuoka, R]]

[[Category: Transport protein]]