2K60
NMR structure of calcium-loaded STIM1 EF-SAM
Summary for 2K60
| Entry DOI | 10.2210/pdb2k60/pdb |
| NMR Information | BMRB: 15851 |
| Descriptor | PROTEIN (Stromal interaction molecule 1), CALCIUM ION (2 entities in total) |
| Functional Keywords | ef-hand, sam domain, ef-sam, stim1, stromal interaction molecule, store operated calcium entry regulator, soce, endoplasmic reticulum luminal calcium sensor, calcium transport, glycoprotein, ion transport, membrane, phosphoprotein, transmembrane, transport, transport protein, signaling protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: Q13586 |
| Total number of polymer chains | 1 |
| Total formula weight | 17420.45 |
| Authors | Stathopulos, P.B.,Ikura, M. (deposition date: 2008-07-02, release date: 2008-10-07, Last modification date: 2024-05-01) |
| Primary citation | Stathopulos, P.B.,Zheng, L.,Li, G.Y.,Plevin, M.J.,Ikura, M. Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell(Cambridge,Mass.), 135:110-122, 2008 Cited by PubMed Abstract: Stromal interaction molecule-1 (STIM1) activates store-operated Ca2+ entry (SOCE) in response to diminished luminal Ca2+ levels. Here, we present the atomic structure of the Ca2+-sensing region of STIM1 consisting of the EF-hand and sterile alpha motif (SAM) domains (EF-SAM). The canonical EF-hand is paired with a previously unidentified EF-hand. Together, the EF-hand pair mediates mutually indispensable hydrophobic interactions between the EF-hand and SAM domains. Structurally critical mutations in the canonical EF-hand, "hidden" EF-hand, or SAM domain disrupt Ca2+ sensitivity in oligomerization via destabilization of the entire EF-SAM entity. In mammalian cells, EF-SAM destabilization mutations within full-length STIM1 induce punctae formation and activate SOCE independent of luminal Ca2+. We provide atomic resolution insight into the molecular basis for STIM1-mediated SOCE initiation and show that the folded/unfolded state of the Ca2+-sensing region of STIM is crucial to SOCE regulation. PubMed: 18854159DOI: 10.1016/j.cell.2008.08.006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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