8IWS
hSPCA1 in the CaE2P state
Summary for 8IWS
| Entry DOI | 10.2210/pdb8iws/pdb |
| EMDB information | 35778 |
| Descriptor | Calcium-transporting ATPase type 2C member 1, MAGNESIUM ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | hspca1, membrane protein, metal transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 100809.39 |
| Authors | |
| Primary citation | Wu, M.,Wu, C.,Song, T.,Pan, K.,Wang, Y.,Liu, Z. Structure and transport mechanism of the human calcium pump SPCA1. Cell Res., 33:533-545, 2023 Cited by PubMed Abstract: Secretory-pathway Ca-ATPases (SPCAs) play critical roles in maintaining Ca homeostasis, but the exact mechanism of SPCAs-mediated Ca transport remains unclear. Here, we determined six cryo-electron microscopy (cryo-EM) structures of human SPCA1 (hSPCA1) in a series of intermediate states, revealing a near-complete conformational cycle. With the aid of molecular dynamics simulations, these structures offer a clear structural basis for Ca entry and release in hSPCA1. We found that hSPCA1 undergoes unique conformational changes during ATP binding and phosphorylation compared to other well-studied P-type II ATPases. In addition, we observed a conformational distortion of the Ca-binding site induced by the separation of transmembrane helices 4L and 6, unveiling a distinct Ca release mechanism. Particularly, we determined a structure of the long-sought CaE2P state of P-type IIA ATPases, providing valuable insights into the Ca transport cycle. Together, these findings enhance our understanding of Ca transport by hSPCA1 and broaden our knowledge of P-type ATPases. PubMed: 37258749DOI: 10.1038/s41422-023-00827-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.42 Å) |
Structure validation
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