5GUG
Crystal structure of inositol 1,4,5-trisphosphate receptor large cytosolic domain with inositol 1,4,5-trisphosphate
Summary for 5GUG
| Entry DOI | 10.2210/pdb5gug/pdb |
| Descriptor | Inositol 1,4,5-trisphosphate receptor type 1, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | receptor channel calcium, metal transport |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Endoplasmic reticulum membrane ; Multi-pass membrane protein : P11881 |
| Total number of polymer chains | 2 |
| Total formula weight | 505594.82 |
| Authors | Hamada, K.,Miyatake, H.,Terauchi, A.,Mikoshiba, K. (deposition date: 2016-08-29, release date: 2017-04-26, Last modification date: 2024-03-20) |
| Primary citation | Hamada, K.,Miyatake, H.,Terauchi, A.,Mikoshiba, K. IP3-mediated gating mechanism of the IP3 receptor revealed by mutagenesis and X-ray crystallography Proc. Natl. Acad. Sci. U.S.A., 114:4661-4666, 2017 Cited by PubMed Abstract: The inositol 1,4,5-trisphosphate (IP) receptor (IPR) is an IP-gated ion channel that releases calcium ions (Ca) from the endoplasmic reticulum. The IP-binding sites in the large cytosolic domain are distant from the Ca conducting pore, and the allosteric mechanism of how IP opens the Ca channel remains elusive. Here, we identify a long-range gating mechanism uncovered by channel mutagenesis and X-ray crystallography of the large cytosolic domain of mouse type 1 IPR in the absence and presence of IP Analyses of two distinct space group crystals uncovered an IP-dependent global translocation of the curvature α-helical domain interfacing with the cytosolic and channel domains. Mutagenesis of the IPR channel revealed an essential role of a leaflet structure in the α-helical domain. These results suggest that the curvature α-helical domain relays IP-controlled global conformational dynamics to the channel through the leaflet, conferring long-range allosteric coupling from IP binding to the Ca channel. PubMed: 28416699DOI: 10.1073/pnas.1701420114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (7.399 Å) |
Structure validation
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