6QWR
Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers
Summary for 6QWR
| Entry DOI | 10.2210/pdb6qwr/pdb |
| Related | 6QAM |
| NMR Information | BMRB: 34365 |
| Descriptor | Outer membrane protein AlkL (1 entity in total) |
| Functional Keywords | outer membrane protein, beta barrel, porin, transporter, membrane protein |
| Biological source | Pseudomonas oleovorans |
| Total number of polymer chains | 1 |
| Total formula weight | 24087.91 |
| Authors | Schubeis, T.,Andreas, L.B.,Pintacuda, G. (deposition date: 2019-03-06, release date: 2020-03-18, Last modification date: 2024-06-19) |
| Primary citation | Schubeis, T.,Le Marchand, T.,Daday, C.,Kopec, W.,Tekwani Movellan, K.,Stanek, J.,Schwarzer, T.S.,Castiglione, K.,de Groot, B.L.,Pintacuda, G.,Andreas, L.B. A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL. Proc.Natl.Acad.Sci.USA, 117:21014-21021, 2020 Cited by PubMed Abstract: The protein AlkL is known to increase permeability of the outer membrane of bacteria for hydrophobic molecules, yet the mechanism of transport has not been determined. Differing crystal and NMR structures of homologous proteins resulted in a controversy regarding the degree of structure and the role of long extracellular loops. Here we solve this controversy by determining the de novo NMR structure in near-native lipid bilayers, and by accessing structural dynamics relevant to hydrophobic substrate permeation through molecular-dynamics simulations and by characteristic NMR relaxation parameters. Dynamic lateral exit sites large enough to accommodate substrates such as carvone or octane occur through restructuring of a barrel extension formed by the extracellular loops. PubMed: 32817429DOI: 10.1073/pnas.2002598117 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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