6BBF
The CRAC channel Orai in an open conformation; H206A gain-of-function mutation
This is a non-PDB format compatible entry.
Summary for 6BBF
| Entry DOI | 10.2210/pdb6bbf/pdb |
| Related | 4HKR |
| Descriptor | Calcium release-activated calcium channel protein 1 (1 entity in total) |
| Functional Keywords | ion channel, calcium, soce, crac, eukaryotic, open structure, membrane protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 24 |
| Total formula weight | 579844.03 |
| Authors | Long, S.B.,Hou, X.,Burstein, S. (deposition date: 2017-10-18, release date: 2018-09-12, Last modification date: 2023-08-16) |
| Primary citation | Hou, X.,Burstein, S.R.,Long, S.B. Structures reveal opening of the store-operated calcium channel Orai. Elife, 7:-, 2018 Cited by PubMed Abstract: The store-operated calcium (Ca) channel Orai governs Ca influx through the plasma membrane of many non-excitable cells in metazoans. The channel opens in response to the depletion of Ca stored in the endoplasmic reticulum (ER). Loss- and gain-of-function mutants of Orai cause disease. Our previous work revealed the structure of Orai with a closed pore. Here, using a gain-of-function mutation that constitutively activates the channel, we present an X-ray structure of Orai in an open conformation. Well-defined electron density maps reveal that the pore is dramatically dilated on its cytosolic side in comparison to the slender closed pore. Cations and anions bind in different regions of the open pore, informing mechanisms for ion permeation and Ca selectivity. Opening of the pore requires the release of cytosolic latches. Together with additional X-ray structures of an unlatched-but-closed conformation, we propose a sequence for store-operated activation. PubMed: 30160233DOI: 10.7554/eLife.36758 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6.706 Å) |
Structure validation
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