6YB1
Crystal structure of an antiparallel octameric transmembrane coiled coil K2-CCTM-VbIc
Summary for 6YB1
| Entry DOI | 10.2210/pdb6yb1/pdb |
| Descriptor | K2-CCTM-VbIc, GLYCINE, NONAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | de novo protein, antiparallel coiled coil, de novo membrane protein, coiled coil |
| Biological source | synthetic construct |
| Total number of polymer chains | 4 |
| Total formula weight | 13261.53 |
| Authors | Kratochvil, H.T.,Liu, L.,Scott, A.J.,Woolfson, D.N.,DeGrado, W.F. (deposition date: 2020-03-15, release date: 2021-04-07, Last modification date: 2024-11-13) |
| Primary citation | Scott, A.J.,Niitsu, A.,Kratochvil, H.T.,Lang, E.J.M.,Sengel, J.T.,Dawson, W.M.,Mahendran, K.R.,Mravic, M.,Thomson, A.R.,Brady, R.L.,Liu, L.,Mulholland, A.J.,Bayley, H.,DeGrado, W.F.,Wallace, M.I.,Woolfson, D.N. Constructing ion channels from water-soluble alpha-helical barrels. Nat.Chem., 13:643-650, 2021 Cited by PubMed Abstract: The design of peptides that assemble in membranes to form functional ion channels is challenging. Specifically, hydrophobic interactions must be designed between the peptides and at the peptide-lipid interfaces simultaneously. Here, we take a multi-step approach towards this problem. First, we use rational de novo design to generate water-soluble α-helical barrels with polar interiors, and confirm their structures using high-resolution X-ray crystallography. These α-helical barrels have water-filled lumens like those of transmembrane channels. Next, we modify the sequences to facilitate their insertion into lipid bilayers. Single-channel electrical recordings and fluorescent imaging of the peptides in membranes show monodisperse, cation-selective channels of unitary conductance. Surprisingly, however, an X-ray structure solved from the lipidic cubic phase for one peptide reveals an alternative state with tightly packed helices and a constricted channel. To reconcile these observations, we perform computational analyses to compare the properties of possible different states of the peptide. PubMed: 33972753DOI: 10.1038/s41557-021-00688-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
Download full validation report
