Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of a sperm-specific solute carrier gated by voltage and cAMP.
Journal, issue, pages	Nature, Vol. 623, Issue 7985, Page 202-209, Year 2023
Publish date	Oct 25, 2023
Authors	Valeria Kalienkova / Martin F Peter / Jan Rheinberger / Cristina Paulino /
PubMed Abstract	The newly characterized sperm-specific Na/H exchanger stands out by its unique tripartite domain composition. It unites a classical solute carrier unit with regulatory domains usually found in ion ...The newly characterized sperm-specific Na/H exchanger stands out by its unique tripartite domain composition. It unites a classical solute carrier unit with regulatory domains usually found in ion channels, namely, a voltage-sensing domain and a cyclic-nucleotide binding domain, which makes it a mechanistic chimera and a secondary-active transporter activated strictly by membrane voltage. Our structures of the sea urchin SpSLC9C1 in the absence and presence of ligands reveal the overall domain arrangement and new structural coupling elements. They allow us to propose a gating model, where movements in the voltage sensor indirectly cause the release of the exchanging unit from a locked state through long-distance allosteric effects transmitted by the newly characterized coupling helices. We further propose that modulation by its ligand cyclic AMP occurs by means of disruption of the cytosolic dimer interface, which lowers the energy barrier for S4 movements in the voltage-sensing domain. As SLC9C1 members have been shown to be essential for male fertility, including in mammals, our structure represents a potential new platform for the development of new on-demand contraceptives.
External links	Nature / PubMed:37880361 / PubMed Central
Methods	EM (single particle)
Resolution	3.05 - 3.74 Å
Structure data	17596 8pcz EMDB-17596, PDB-8pcz: Ligand-free SpSLC9C1 in lipid nanodiscs, dimer Method: EM (single particle) / Resolution: 3.21 Å 17598 8pd2 EMDB-17598, PDB-8pd2: Ligand-free SpSLC9C1 in lipid nanodiscs, protomer state 1 Method: EM (single particle) / Resolution: 3.25 Å 17599 8pd3 EMDB-17599, PDB-8pd3: Ligand-free SpSLC9C1 in lipid nanodiscs, protomer state 2 Method: EM (single particle) / Resolution: 3.3 Å 17601 8pd5 EMDB-17601, PDB-8pd5: Ligand-free SpSLC9C1 in lipid nanodiscs, protomer state 3 Method: EM (single particle) / Resolution: 3.4 Å 17602 8pd7 EMDB-17602, PDB-8pd7: Ligand-free SpSLC9C1 in lipid nanodiscs, protomer state 4 Method: EM (single particle) / Resolution: 3.4 Å EMDB-17603: Ligand-free SpSLC9C1 in detergent, asymmetric class Method: EM (single particle) / Resolution: 3.3 Å EMDB-17604: Ligand-free SpSLC9C1 in detergent, symmetric class Method: EM (single particle) / Resolution: 3.05 Å 17605 8pd8 EMDB-17605, PDB-8pd8: cAMP-bound SpSLC9C1 in lipid nanodiscs, dimer Method: EM (single particle) / Resolution: 3.3 Å 17607 8pd9 EMDB-17607, PDB-8pd9: cAMP-bound SpSLC9C1 in lipid nanodiscs, protomer state 1 Method: EM (single particle) / Resolution: 3.6 Å 17621 8pdu EMDB-17621, PDB-8pdu: cGMP-bound SpSLC9C1 in lipid nanodiscs, dimer Method: EM (single particle) / Resolution: 3.22 Å 17622 8pdv EMDB-17622, PDB-8pdv: cGMP-bound SpSLC9C1 in lipid nanodiscs, protomer Method: EM (single particle) / Resolution: 3.26 Å EMDB-17625: cAMP-bound SpSLC9C1 in lipid nanodiscs, protomer state 2 Method: EM (single particle) / Resolution: 3.74 Å
Chemicals	ChemComp-CMP: ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE / Cyclic adenosine monophosphate ChemComp-PCG: CYCLIC GUANOSINE MONOPHOSPHATE / Cyclic guanosine monophosphate
Source	strongylocentrotus purpuratus (purple sea urchin)
Keywords	MEMBRANE PROTEIN / SLC9 / NHE / sperm-specific