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A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins (2008)

by J P Renn, P L Clark
Venue:Biopolymers
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1.1. The Autotransporter Pathway

by Serine Protease, Autotransporters Enterobacteriaceae, Spates) Biogenesis, Nathalie Dautin , 2010
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...orming aggregates [52]. However, this does not appear to be specific to AT missing the N-terminal extension, since the folding of the SPATE Pet was not significantly different from Pertactin in vitro =-=[53]-=-. In vitro folding is nevertheless very different from in vivo events, where secreted proteins might encounter chaperones in the periplasm. Indeed, two SPATE “stalled” mutants have recently been used ...

virulence

by Mirco Junker, Richard N. Besingi, Patricia L. Clark
"... transport and folding of an autotransporter ..."
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transport and folding of an autotransporter
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...al structure in the passenger domains of Bordetella pertussis pertactin and Escherichia coli Pet are markedly more stable than the N-terminal portions of these passenger domains (Junker et al., 2006; =-=Renn and Clark, 2008-=-). These results led us to propose a model for AT OM secretion in which the free Fig. 1. AT OM secretion models, and design of stalled constructs. A. Three models for OM secretion of AT proteins: vect...

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