6qwr | pdb_00006qwr

Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers

spinqualitylabelsall models 6qwr Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qwr is a 1 chain structure with sequence from Pseudomonas oleovorans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALKL_PSEOL Could be involved in the transport of substrates. Publication Abstract from PubMed 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. A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.,Schubeis T, Le Marchand T, Daday C, Kopec W, Tekwani Movellan K, Stanek J, Schwarzer TS, Castiglione K, de Groot BL, Pintacuda G, Andreas LB Proc Natl Acad Sci U S A. 2020 Aug 19. pii: 2002598117. doi:, 10.1073/pnas.2002598117. PMID:32817429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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