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TitleStructure, mechanism and lipid-mediated remodeling of the mammalian Na/H exchanger NHA2.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 2, Page 108-120, Year 2022
Publish dateFeb 16, 2022
AuthorsRei Matsuoka / Roman Fudim / Sukkyeong Jung / Chenou Zhang / Andre Bazzone / Yurie Chatzikyriakidou / Carol V Robinson / Norimichi Nomura / So Iwata / Michael Landreh / Laura Orellana / Oliver Beckstein / David Drew /
PubMed AbstractThe 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 ...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 Å 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.
External linksNat Struct Mol Biol / PubMed:35173351 / PubMed Central
MethodsEM (single particle)
Resolution3.04 - 3.64 Å
Structure data

EMDB-13161, PDB-7p1i:
Cryo EM structure of bison NHA2 in detergent and N-terminal extension helix
Method: EM (single particle) / Resolution: 3.15 Å

EMDB-13162, PDB-7p1j:
Cryo EM structure of bison NHA2 in detergent structure
Method: EM (single particle) / Resolution: 3.04 Å

EMDB-13163, PDB-7p1k:
Cryo EM structure of bison NHA2 in nano disc structure
Method: EM (single particle) / Resolution: 3.64 Å

EMDB-13597:
Cryo EM map of bison NHA2 in detergent structure
Method: EM (single particle) / Resolution: 3.04 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-T7X:
Phosphatidylinositol / Phosphatidylinositol

Source
  • bison bison (American bison)
KeywordsTRANSPORT PROTEIN / Membrane protein Sodium proton transporter

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