Structure of outer membrane protein G in lipid bilayers

被引：87

作者：

Retel, Joren S. ^{[1
]}

Nieuwkoop, Andrew J. ^{[1
]}

Hiller, Matthias ^{[1
]}

Higman, Victoria A. ^{[1
]}

Barbet-Massin, Emeline ^{[2
]}

Stanek, Jan ^{[2
]}

Andreas, Loren B. ^{[2
]}

Franks, W. Trent ^{[1
]}

van Rossum, Barth-Jan ^{[1
]}

Vinothkumar, Kutti R. ^{[3
]}

Handel, Lieselotte ^{[1
]}

de Palma, Gregorio Giuseppe ^{[1
]}

Bardiaux, Benjamin ^{[1
,4
]}

Pintacuda, Guido ^{[2
]}

Emsley, Lyndon ^{[2
,5
]}

Kuehlbrandt, Werner ^{[3
]}

Oschkinat, Hartmut ^{[1
]}

机构：

[1] Leibniz Inst Mol Pharmacol, Robert Rossle Str 10, D-13125 Berlin, Germany

[2] Univ Lyon, Ctr RMN Tres Hauts Champs, Inst Sci Analyt, CNRS,ENS Lyon,UCB Lyon 1, F-69100 Villeurbanne, France

[3] Max Planck Inst Biophys, Max Von Laue Str 3, D-60438 Frankfurt, Germany

[4] Inst Pasteur, CNRS, UMR 3528, Unite Bioinformat Struct, F-75015 Paris, France

[5] Ecole Polytech Fed Lausanne, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland

来源：

NATURE COMMUNICATIONS | 2017年 / 8卷

关键词：

SOLID-STATE NMR; AUTOMATED NOE ASSIGNMENT; ESCHERICHIA-COLI K-12; MONOMERIC PORIN OMPG; ANGLE-SPINNING NMR; RESONANCE ASSIGNMENT; RECOMBINANT PROTEINS; TORSION ANGLES; C-13; SPECTROSCOPY;

D O I：

10.1038/s41467-017-02228-2

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

beta-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-1-H-1 and C-13-C-13 distance restraints, 256 torsion angles, but no hydrogen bond restraints are used to calculate the structure. The length of beta-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.

引用

页数：10

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