5L24
Structure of CNTnw N149L in the intermediate 2 state
Summary for 5L24
Entry DOI | 10.2210/pdb5l24/pdb |
Related | 5L26 5L27 5L28 5L29 5L2A 5L2B |
Descriptor | Nucleoside permease, 2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}-2-octyldecyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside (2 entities in total) |
Functional Keywords | transporter, nucleoside, elevator-type alternate access, transport protein |
Biological source | Neisseria wadsworthii 9715 |
Total number of polymer chains | 3 |
Total formula weight | 135918.97 |
Authors | Hirschi, M.,Johnson, Z.L.,Lee, S.-Y. (deposition date: 2016-07-31, release date: 2017-04-12, Last modification date: 2023-10-04) |
Primary citation | Hirschi, M.,Johnson, Z.L.,Lee, S.Y. Visualizing multistep elevator-like transitions of a nucleoside transporter. Nature, 545:66-70, 2017 Cited by PubMed Abstract: Membrane transporters move substrates across the membrane by alternating access of their binding sites between the opposite sides of the membrane. An emerging model of this process is the elevator mechanism, in which a substrate-binding transport domain moves a large distance across the membrane. This mechanism has been characterized by a transition between two states, but the conformational path that leads to the transition is not yet known, largely because the available structural information has been limited to the two end states. Here we present crystal structures of the inward-facing, intermediate, and outward-facing states of a concentrative nucleoside transporter from Neisseria wadsworthii. Notably, we determined the structures of multiple intermediate conformations, in which the transport domain is captured halfway through its elevator motion. Our structures present a trajectory of the conformational transition in the elevator model, revealing multiple intermediate steps and state-dependent conformational changes within the transport domain that are associated with the elevator-like motion. PubMed: 28424521DOI: 10.1038/nature22057 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
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