Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins

Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins

Abstract Pore-forming repeats in toxins (RTX) are key virulence factors of many Gram-negative pathogens. We have recently shown that the aromatic side chain of the conserved tyrosine residue 940 within the acylated segment of the RTX adenylate cyclase toxin-hemolysin (CyaA, ACT or AC-Hly) plays a ke...

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Autores principales: Anna Lepesheva, Adriana Osickova, Jana Holubova, David Jurnecka, Sarka Knoblochova, Carlos Espinosa-Vinals, Ladislav Bumba, Karolina Skopova, Radovan Fiser, Radim Osicka, Peter Sebo, Jiri Masin
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Medicine
R
Science
Q
Acceso en línea:https://doaj.org/article/6f873568b2e4490a9da5948d8fb80b36
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