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  Solid-state NMR study of the YadA membrane-anchor domain in the bacterial outer membrane.

Shahid, S. A., Nagaraj, M., Chauhan, N., Franks, T. W., Bardiaux, B., Habeck, M., et al. (2015). Solid-state NMR study of the YadA membrane-anchor domain in the bacterial outer membrane. Angewandte Chemie-International Edition, 54(43), 12602-12606. doi:10.1002/anie.201505506.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-059C-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-05A0-B
Genre: Journal Article

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 Creators:
Shahid, S. A., Author
Nagaraj, M., Author
Chauhan, N., Author
Franks, T. W., Author
Bardiaux, B., Author
Habeck, M.1, Author              
Orwick-Rydmark, M., Author
Linke, D., Author
van Rossum, B. J., Author
Affiliations:
1Research Group of Statistical Inverse-Problems in Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_1113580              

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 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 13C-13C 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 membrane environments.

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Language(s): eng - English
 Dates: 2015-08-312015-10-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201505506
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Title: Angewandte Chemie-International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 54 (43) Sequence Number: - Start / End Page: 12602 - 12606 Identifier: -