| http://purl.uniprot.org/citations/31626806 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31626806 | http://www.w3.org/2000/01/rdf-schema#comment | "Store operated calcium (Ca2+) entry (SOCE) is the process whereby endoplasmic reticulum (ER) Ca2+ store depletion causes Orai1-composed Ca2+ channels on the plasma membrane (PM) to open, mediating a rise in cytosolic Ca2+ levels. Stromal interaction molecules (STIMs) are the proteins that directly sense ER Ca2+ content and gate Orai1 channels due to store depletion. The trigger for STIM activation is Ca2+ unbinding from the ER lumen-oriented domains, which consist of a nonconserved amino (N) terminal region and EF-hand and sterile α motif (SAM) domains (EF-SAM), highly conserved from humans to Caenorhabditis elegans. Solution NMR structures of the human EF-SAM domains have been determined at high Ca2+ concentrations; however, no direct structural view of the Ca2+ binding mode has been elucidated. Further, no atomic resolution data currently exists on EF-SAM at low Ca2+ levels. Here, we determined the X-ray crystal structure of the C. elegans STIM luminal domain, revealing that EF-SAM binds a single Ca2+ ion with pentagonal bipyramidal geometry and an ancillary α-helix formed by the N-terminal region acts as a brace to stabilize EF-SAM. Using solution NMR, we observed EF-hand domain unfolding and a conformational exchange between folded and unfolded states involving the ancillary α-helix and the canonical EF-hand in low Ca2+. Remarkably, we also detected an α-helix (+Ca2+) to β-strand (-Ca2+) transition at the terminal SAM domain α-helix. Collectively, our analyses indicate that one canonically bound Ca2+ ion is sufficient to stabilize the quiescent luminal domain structure, precluding unfolding, conformational exchange, and secondary structure transformation."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2019.10.003"xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Nishikawa T."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Zheng L."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Ikura M."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Ishiyama N."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Enomoto M."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Stathopulos P.B."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/author | "Back S.I."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/pages | "367-383"xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/title | "Coordination of a Single Calcium Ion in the EF-hand Maintains the Off State of the Stromal Interaction Molecule Luminal Domain."xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://purl.uniprot.org/core/volume | "432"xsd:string |
| http://purl.uniprot.org/citations/31626806 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31626806 |
| http://purl.uniprot.org/citations/31626806 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31626806 |
| http://purl.uniprot.org/uniprot/#_G5EF60-mappedCitation-31626806 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31626806 |
| http://purl.uniprot.org/uniprot/G5EF60 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/31626806 |