Structure of outer membrane protein G in lipid bilayers

Joren S. Retel; Andrew J. Nieuwkoop; Matthias Hiller; Victoria A. Higman; Emeline Barbet-Massin; Jan Stanek; Loren B. Andreas; W. Trent Franks; Barth-Jan Rossum; Kutti R. Vinothkumar; Lieselotte Handel; Gregorio Giuseppe Palma; Benjamin Bardiaux; Guido Pintacuda; Lyndon Emsley; Werner Kühlbrandt; Hartmut Oschkinat

doi:10.1038/s41467-017-02228-2

Structure of outer membrane protein G in lipid bilayers

Joren S. Retel
, Andrew J. Nieuwkoop
, Matthias Hiller
, Victoria A. Higman
, Emeline Barbet-Massin
, Jan Stanek
, Loren B. Andreas
, W. Trent Franks
, Barth-Jan Rossum
, Kutti R. Vinothkumar
, Lieselotte Handel
, Gregorio Giuseppe Palma
, Benjamin Bardiaux
, Guido Pintacuda
, Lyndon Emsley
, Werner Kühlbrandt
, Hartmut Oschkinat

School of Chemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

104 Citations (Scopus)

Abstract

Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.

Original language	English
Pages (from-to)	2073
Number of pages	1
Journal	Nature Communications
Volume	8
DOIs	https://doi.org/10.1038/s41467-017-02228-2
Publication status	Published - 12 Dec 2017

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Retel, J. S., Nieuwkoop, A. J., Hiller, M., Higman, V. A., Barbet-Massin, E., Stanek, J., Andreas, L. B., Franks, W. T., Rossum, B.-J., Vinothkumar, K. R., Handel, L., Palma, G. G., Bardiaux, B., Pintacuda, G., Emsley, L., Kühlbrandt, W., & Oschkinat, H. (2017). Structure of outer membrane protein G in lipid bilayers. Nature Communications, 8, 2073. https://doi.org/10.1038/s41467-017-02228-2

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title = "Structure of outer membrane protein G in lipid bilayers",

abstract = "Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.",

author = "Retel, \{Joren S.\} and Nieuwkoop, \{Andrew J.\} and Matthias Hiller and Higman, \{Victoria A.\} and Emeline Barbet-Massin and Jan Stanek and Andreas, \{Loren B.\} and Franks, \{W. Trent\} and Barth-Jan Rossum and Vinothkumar, \{Kutti R.\} and Lieselotte Handel and Palma, \{Gregorio Giuseppe\} and Benjamin Bardiaux and Guido Pintacuda and Lyndon Emsley and Werner K{\"u}hlbrandt and Hartmut Oschkinat",

year = "2017",

month = dec,

day = "12",

doi = "10.1038/s41467-017-02228-2",

language = "English",

volume = "8",

pages = "2073",

journal = "Nature Communications",

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Retel, JS, Nieuwkoop, AJ, Hiller, M, Higman, VA, Barbet-Massin, E, Stanek, J, Andreas, LB, Franks, WT, Rossum, B-J, Vinothkumar, KR, Handel, L, Palma, GG, Bardiaux, B, Pintacuda, G, Emsley, L, Kühlbrandt, W & Oschkinat, H 2017, 'Structure of outer membrane protein G in lipid bilayers', Nature Communications, vol. 8, pp. 2073. https://doi.org/10.1038/s41467-017-02228-2

TY - JOUR

T1 - Structure of outer membrane protein G in lipid bilayers

AU - Retel, Joren S.

AU - Nieuwkoop, Andrew J.

AU - Hiller, Matthias

AU - Higman, Victoria A.

AU - Barbet-Massin, Emeline

AU - Stanek, Jan

AU - Andreas, Loren B.

AU - Franks, W. Trent

AU - Rossum, Barth-Jan

AU - Vinothkumar, Kutti R.

AU - Handel, Lieselotte

AU - Palma, Gregorio Giuseppe

AU - Bardiaux, Benjamin

AU - Pintacuda, Guido

AU - Emsley, Lyndon

AU - Kühlbrandt, Werner

AU - Oschkinat, Hartmut

PY - 2017/12/12

Y1 - 2017/12/12

N2 - Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.

AB - Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.

U2 - 10.1038/s41467-017-02228-2

DO - 10.1038/s41467-017-02228-2

M3 - Article (Academic Journal)

C2 - 29233991

SN - 2041-1723

VL - 8

SP - 2073

JO - Nature Communications

JF - Nature Communications

ER -

Structure of outer membrane protein G in lipid bilayers

Abstract

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