4D0A
3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii
Summary for 4D0A
| Entry DOI | 10.2210/pdb4d0a/pdb |
| EMDB information | 2636 |
| Descriptor | NA(+)/H(+) ANTIPORTER 1 (1 entity in total) |
| Functional Keywords | transport protein, membrane protein, antiporter, transporter, exchanger, cpa |
| Biological source | METHANOCALDOCOCCUS JANNASCHII DSM 2661 |
| Cellular location | Cell membrane ; Multi-pass membrane protein : Q60362 |
| Total number of polymer chains | 1 |
| Total formula weight | 45998.89 |
| Authors | Paulino, C.,Woehlert, D.,Yildiz, O.,Kuhlbrandt, W. (deposition date: 2014-04-25, release date: 2014-12-10, Last modification date: 2023-12-20) |
| Primary citation | Paulino, C.,Woehlert, D.,Yildiz, O.,Kuhlbrandt, W. 3D Em Map of the Sodium Proton Antiporter Mjnhap1 from Methanocaldococcus Jannaschii Elife, 3:-, 2014 Cited by PubMed Abstract: Sodium/proton antiporters are essential for sodium and pH homeostasis and play a major role in human health and disease. We determined the structures of the archaeal sodium/proton antiporter MjNhaP1 in two complementary states. The inward-open state was obtained by x-ray crystallography in the presence of sodium at pH 8, where the transporter is highly active. The outward-open state was obtained by electron crystallography without sodium at pH 4, where MjNhaP1 is inactive. Comparison of both structures reveals a 7° tilt of the 6 helix bundle. (22)Na(+) uptake measurements indicate non-cooperative transport with an activity maximum at pH 7.5. We conclude that binding of a Na(+) ion from the outside induces helix movements that close the extracellular cavity, open the cytoplasmic funnel, and result in a ∼5 Å vertical relocation of the ion binding site to release the substrate ion into the cytoplasm. PubMed: 25426803DOI: 10.7554/ELIFE.03583 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (6 Å) |
Structure validation
Download full validation report
