8JBK
Crystal structure of Na+,K+-ATPase in the E1.3Na+ state
Summary for 8JBK
| Entry DOI | 10.2210/pdb8jbk/pdb |
| Descriptor | Sodium/potassium-transporting ATPase subunit alpha, 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (14 entities in total) |
| Functional Keywords | ion pump, p-type atpase, membrane protein |
| Biological source | Sus scrofa (pig) More |
| Total number of polymer chains | 6 |
| Total formula weight | 330245.49 |
| Authors | Kanai, R.,Vilsen, B.,Cornelius, F.,Toyoshima, C. (deposition date: 2023-05-09, release date: 2023-08-09, Last modification date: 2024-11-13) |
| Primary citation | Kanai, R.,Vilsen, B.,Cornelius, F.,Toyoshima, C. Crystal structures of Na + ,K + -ATPase reveal the mechanism that converts the K + -bound form to Na + -bound form and opens and closes the cytoplasmic gate. Febs Lett., 597:1957-1976, 2023 Cited by PubMed Abstract: Na ,K -ATPase (NKA) plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane by alternating between the E1 (showing high affinity for Na and low affinity for K ) and E2 (low affinity to Na and high affinity to K ) forms. Presented here are two crystal structures of NKA in E1·Mg and E1·3Na states at 2.9 and 2.8 Å resolution, respectively. These two E1 structures fill a gap in our description of the NKA reaction cycle based on the atomic structures. We describe how NKA converts the K -bound E2·2K form to an E1 (E1·Mg ) form, which allows high-affinity Na binding, eventually closing the cytoplasmic gate (in E1 ~ P·ADP·3Na ) after binding three Na , while keeping the extracellular ion pathway sealed. We now understand previously unknown functional roles for several parts of NKA and that NKA uses even the lipid bilayer for gating the ion pathway. PubMed: 37357620DOI: 10.1002/1873-3468.14689 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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