2012
DOI: 10.1038/srep00803
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Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR

Abstract: We report the complete solid-state MAS NMR resonance assignment of a medium-sized, trimeric membrane protein, YadA-M. The protein YadA (Yersinia adhesin A) is an important virulence factor of enteropathogenic Yersinia species (such as Yersinia enterocolitica and Yersinia pseudotuberculosis). YadA is localized on the bacterial cell surface and is involved in adhesion to host cells and tissues. It is anchored in the outer membrane by a transmembrane anchor domain (YadA-M). This domain hosts the so-called autotra… Show more

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Cited by 26 publications
(16 citation statements)
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“…When conditions are suitable, cells strengthen their attachment and divide to form a growing population on the surface (O’Toole et al 2000). Attachment is facilitated by a range of secreted products, including polysaccharides, proteins, nucleic acids, and amyloids (Absalon et al 2011, Garcia et al 2011, Linke et al 2006, Ma et al 2006, Romero et al 2010, Shahid, Bardiaux, Franks, Krabben, Habeck, van Rossum & Linke 2012, Shahid, Markovic, Linke & van Rossum 2012, Timmerman et al 1991, Veenstra et al 1996). …”
Section: Introductionmentioning
confidence: 99%
“…When conditions are suitable, cells strengthen their attachment and divide to form a growing population on the surface (O’Toole et al 2000). Attachment is facilitated by a range of secreted products, including polysaccharides, proteins, nucleic acids, and amyloids (Absalon et al 2011, Garcia et al 2011, Linke et al 2006, Ma et al 2006, Romero et al 2010, Shahid, Bardiaux, Franks, Krabben, Habeck, van Rossum & Linke 2012, Shahid, Markovic, Linke & van Rossum 2012, Timmerman et al 1991, Veenstra et al 1996). …”
Section: Introductionmentioning
confidence: 99%
“…High quality solid-state NMR spectra have been reported for samples of membrane proteins in proteolipid 2D crystals, precipitates, and microcrystals (Andreas et al 2015; Barbet-Massin et al 2014; Eddy et al 2012; Li et al 2007; Linser et al 2011; Saurel et al 2017; Shahid et al 2012). These samples, prepared with lipid to protein molecular ratios in the range of 6:1 and 25:1, have the advantage that large quantities of protein can be packed in the NMR rotor for enhanced sensitivity.…”
mentioning
confidence: 99%
“…These pores act as channels for transporting the three N-terminal a-helices passenger domains through the bacterial outer membrane (Roggenkamp et al 2003;Oomen et al 2004;Surana et al 2004;Meng et al 2006). Shahid et al predicted the secondary sturcture of YadA-M by taking advantage of solid-state magic-angle spinning (MAS) NMR and indicated that this domain contains a number of amphipathic, antiparallel b-strands, at both ends of these b-strands are frequently made from aromatic residues that interact with the water-lipid interface to anchor the TAAs in the lipid membrane (Shahid et al 2012). …”
Section: The Common Molecular Structures Of Taasmentioning
confidence: 98%