3UU3
The GLIC pentameric Ligand-Gated Ion Channel Loop2-20' oxidized mutant in a locally-closed conformation (LC1 subtype)
Summary for 3UU3
| Entry DOI | 10.2210/pdb3uu3/pdb |
| Related | 3TLS 3TLT 3TLU 3TLV 3TLW 3UU4 3UU5 3UU6 3UU8 3UUB |
| Descriptor | Glr4197 protein, DODECYL-BETA-D-MALTOSIDE (3 entities in total) |
| Functional Keywords | cys-loop receptor family, membrane protein, transport protein |
| Biological source | Gloeobacter violaceus |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (Probable): Q7NDN8 |
| Total number of polymer chains | 5 |
| Total formula weight | 183200.50 |
| Authors | Sauguet, L.,Nury, H.,Corringer, P.J.,Delarue, M. (deposition date: 2011-11-28, release date: 2012-05-16, Last modification date: 2023-09-13) |
| Primary citation | Prevost, M.S.,Sauguet, L.,Nury, H.,Van Renterghem, C.,Huon, C.,Poitevin, F.,Baaden, M.,Delarue, M.,Corringer, P.J. A locally closed conformation of a bacterial pentameric proton-gated ion channel. Nat.Struct.Mol.Biol., 19:642-649, 2012 Cited by PubMed Abstract: Pentameric ligand-gated ion channels mediate signal transduction through conformational transitions between closed-pore and open-pore states. To stabilize a closed conformation of GLIC, a bacterial proton-gated homolog from Gloeobacter violaceus whose open structure is known, we separately generated either four cross-links or two single mutations. We found all six mutants to be in the same 'locally closed' conformation using X-ray crystallography, sharing most of the features of the open form but showing a locally closed pore as a result of a concerted bending of all of its M2 helices. The mutants adopt several variant conformations of the M2-M3 loop, and in all cases an interacting lipid that is observed in the open form disappears. A single cross-linked mutant is functional, according to electrophysiology, and the locally closed structure of this mutant indicates that it has an increased flexibility. Further cross-linking, accessibility and molecular dynamics data suggest that the locally closed form is a functionally relevant conformation that occurs during allosteric gating transitions. PubMed: 22580559DOI: 10.1038/nsmb.2307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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