5MWV

Solid-state NMR Structure of outer membrane protein G in lipid bilayers

Summary for 5MWV

• Entry DOI: 10.2210/pdb5mwv/pdb
• NMR Information: BMRB: 34088
• Descriptor: Outer membrane protein G (1 entity in total)
• Functional Keywords: porin beta-barrel membrane lipid, membrane protein
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 32936.53

Authors

Retel, J.S.,Nieuwkoop, A.J.,Hiller, M.,Higman, V.A.,Barbet-Massin, E.,Stanek, J.,Andreas, L.B.,Franks, W.T.,van Rossum, B.-J.,Vinothkumar, K.R.,Handel, L.,de Palma, G.G.,Bardiaux, B.,Pintacuda, G.,Emsley, L.,Kuelbrandt, W.,Oschkinat, H. (deposition date: 2017-01-20, release date: 2017-12-27, Last modification date: 2024-05-15)

Primary citation

Retel, J.S.,Nieuwkoop, A.J.,Hiller, M.,Higman, V.A.,Barbet-Massin, E.,Stanek, J.,Andreas, L.B.,Franks, W.T.,van Rossum, B.J.,Vinothkumar, K.R.,Handel, L.,de Palma, G.G.,Bardiaux, B.,Pintacuda, G.,Emsley, L.,Kuhlbrandt, W.,Oschkinat, H.
Structure of outer membrane protein G in lipid bilayers.
Nat Commun, 8:2073-2073, 2017

PubMed Abstract: β-barrel proteins mediate nutrient uptake in bacteria and serve vital functions in cell signaling and adhesion. For the 14-strand outer membrane protein G of Escherichia coli, opening and closing is pH-dependent. Different roles of the extracellular loops in this process were proposed, and X-ray and solution NMR studies were divergent. Here, we report the structure of outer membrane protein G investigated in bilayers of E. coli lipid extracts by magic-angle-spinning NMR. In total, 1847 inter-residue H-H and C-C distance restraints, 256 torsion angles, but no hydrogen bond restraints are used to calculate the structure. The length of β-strands is found to vary beyond the membrane boundary, with strands 6-8 being the longest and the extracellular loops 3 and 4 well ordered. The site of barrel closure at strands 1 and 14 is more disordered than most remaining strands, with the flexibility decreasing toward loops 3 and 4. Loop 4 presents a well-defined helix.

PubMed: 29233991
DOI: 10.1038/s41467-017-02228-2

Experimental method

SOLID-STATE NMR