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  Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)

Chauhan, N., Hatlem, D., Orwick-Rydmark, M., Schneider, K., Floetenmeyer, M., van Rossum, B., et al. (2019). Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA). Molecular Microbiology, 111(3), 844-862. doi:10.1111/mmi.14195.

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Chauhan, N1, Autor           
Hatlem, D, Autor
Orwick-Rydmark, M, Autor
Schneider, K, Autor
Floetenmeyer, M2, Autor           
van Rossum, B, Autor
Leo, JC1, Autor           
Linke, D1, Autor           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_3375791              
2Electron Microscopy, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375794              

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 Zusammenfassung: Trimeric autotransporter adhesins (TAAs) are a subset of a larger protein family called the type V secretion systems. They are localized on the cell surface of Gram-negative bacteria, function as mediators of attachment to inorganic surfaces and host cells, and thus include important virulence factors. Yersinia adhesin A (YadA) from Yersinia enterocolitica is a prototypical TAA that is used extensively to study the structure and function of the type Vc secretion system. A solid-state NMR study of the membrane anchor domain of YadA previously revealed a flexible stretch of small residues, termed the ASSA region, that links the membrane anchor to the stalk domain. In this study, we present evidence that single amino acid proline substitutions produce two different conformers of the membrane anchor domain of YadA; one with the N-termini facing the extracellular surface, and a second with the N-termini located in the periplasm. We propose that TAAs adopt a hairpin intermediate during secretion, as has been shown before for other subtypes of the type V secretion system. As the YadA transition state intermediate can be isolated from the outer membrane, future structural studies should be possible to further unravel details of the autotransport process.

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 Datum: 2019-03
 Publikationsstatus: Erschienen
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 Identifikatoren: DOI: 10.1111/mmi.14195
PMID: 30600549
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Titel: Molecular Microbiology
  Andere : Mol. Microbiol.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Oxford : Blackwell Science
Seiten: - Band / Heft: 111 (3) Artikelnummer: - Start- / Endseite: 844 - 862 Identifikator: ISSN: 0950-382X
CoNE: https://pure.mpg.de/cone/journals/resource/954925574950