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High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles

Artikel i vetenskaplig tidskrift
Författare Johannes Thoma
Björn Marcus Burmann
Publicerad i Biochemistry
Volym 59
Nummer/häfte 17
Sidor 1656-1660
ISSN 0006-2960
Publiceringsår 2020
Publicerad vid Institutionen för kemi och molekylärbiologi
Wallenberg Centre for Molecular and Translational Medicine
Sidor 1656-1660
Språk en
Länkar dx.doi.org/10.1021/acs.biochem.9b01...
Ämnesord escherichia-coli, domain, Biochemistry & Molecular Biology
Ämneskategorier Biokemi och molekylärbiologi

Sammanfattning

The cell envelope of Gram-negative bacteria is an elaborate cellular environment, consisting of two lipid membranes separated by the aqueous periplasm. So far, efforts to mimic this environment under laboratory conditions have been limited by the complexity of the asymmetric bacterial outer membrane. To evade this impasse, we recently established a method to modify the protein composition of bacterial outer membrane vesicles (OMVs) released from Escherichia coli as a platform for biophysical studies of outer membrane proteins in their native membrane environment. Here, we apply protein-enriched OMVs to characterize the structure of three envelope proteins from E. coil using nuclear magnetic resonance (NMR) spectroscopy and expand the methodology to soluble periplasmic proteins. We obtain high-resolution in situ NMR spectra of the transmembrane protein OmpA as well as the periplasmic proteins CpxP and MalE. We find that our approach facilitates structural investigations of membrane-attached protein domains and is especially suited for soluble proteins within their native periplasmic environment. Thereby, the use of OMVs in solution NMR methods allows in situ analysis of the structure and dynamics of proteins twice the size compared to the current in-cell NMR methodology. We therefore expect our work to pave the way for more complex NMR studies of bacterial envelope proteins in the native environment of OMVs in the future.

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