Solid-state NMR Study of the YadA Membrane-Anchor Domain in the Bacterial Outer Membrane

Angewandte Chemie
Shakeel Ahmad ShahidBarth-J van Rossum

Abstract

MAS-NMR was used to study the structure and dynamics at ambient temperatures of the membrane-anchor domain of YadA (YadA-M) in a pellet of the outer membrane of E. coli in which it was expressed. YadA is an adhesin from the pathogen Yersinia enterocolitica that is involved in interactions with the host cell, and it is a model protein for studying the autotransport process. Existing assignments were sucessfully transferred to a large part of the YadA-M protein in the E. coli lipid environment by using (13) C-(13) C DARR and PDSD spectra at different mixing times. The chemical shifts in most regions of YadA-M are unchanged relative to those in microcrystalline YadA-M preparations from which a structure has previously been solved, including the ASSA region that is proposed to be involved in transition-state hairpin formation for transport of the soluble domain. Comparisons of the dynamics between the microcrystalline and membrane-embedded samples indicate greater flexibility of the ASSA region in the outer-membrane preparation at physiological temperatures. This study will pave the way towards MAS-NMR structure determination of membrane proteins, and a better understanding of functionally important dynamic residues in native membr...Continue Reading

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Citations

Sep 24, 2016·Quarterly Reviews of Biophysics·Mohammed KaplanMarc Baldus
Sep 28, 2016·Angewandte Chemie·João Medeiros-SilvaMarkus Weingarth
Nov 23, 2017·Frontiers in Cellular and Infection Microbiology·Ina MeuskensJack C Leo
Dec 29, 2020·Biophysical Journal·James E KentFrancesca M Marassi
May 26, 2018·Journal of the American Chemical Society·Yongxiang ZhaoJun Yang

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