7UGX
Asp-bound GltPh RSMR mutant in IFS-B1 state
Summary for 7UGX
Entry DOI | 10.2210/pdb7ugx/pdb |
EMDB information | 26498 |
Descriptor | Glutamate transporter homolog, ASPARTIC ACID, SODIUM ION (3 entities in total) |
Functional Keywords | gltph, glutamate transporter, substrate, transport protein |
Biological source | Pyrococcus horikoshii |
Total number of polymer chains | 1 |
Total formula weight | 44335.30 |
Authors | Huang, Y.,Boudker, O. (deposition date: 2022-03-25, release date: 2023-03-29, Last modification date: 2023-05-10) |
Primary citation | Huang, Y.,Reddy, K.D.,Bracken, C.,Qiu, B.,Zhan, W.,Eliezer, D.,Boudker, O. Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19 F NMR and Cryo-EM. J.Am.Chem.Soc., 145:8583-8592, 2023 Cited by PubMed Abstract: Limited chemical shift dispersion represents a significant barrier to studying multistate equilibria of large membrane proteins by F NMR. We describe a novel monofluoroethyl F probe that dramatically increases the chemical shift dispersion. The improved conformational sensitivity and line shape enable the detection of previously unresolved states in one-dimensional (1D) F NMR spectra of a 134 kDa membrane transporter. Changes in the populations of these states in response to ligand binding, mutations, and temperature correlate with population changes of distinct conformations in structural ensembles determined by single-particle cryo-electron microscopy (cryo-EM). Thus, F NMR can guide sample preparation to discover and visualize novel conformational states and facilitate image analysis and three-dimensional (3D) classification. PubMed: 37023263DOI: 10.1021/jacs.3c01003 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.96 Å) |
Structure validation
Download full validation report