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• W1991736406 abstract "Autotransporters are virulence factors produced by Gram-negative bacteria. They consist of two domains, an N-terminal 'passenger' domain and a C-terminal beta-domain. beta-domains form beta-barrel structures in the outer membrane while passenger domains are translocated into the extracellular space. In some autotransporters, the two domains are separated by proteolytic cleavage. Using X-ray crystallography, we solved the 2.7-A structure of the post-cleavage state of the beta-domain of EspP, an autotransporter produced by Escherichia coli strain O157:H7. The structure consists of a 12-stranded beta-barrel with the passenger domain-beta-domain cleavage junction located inside the barrel pore, approximately midway between the extracellular and periplasmic surfaces of the outer membrane. The structure reveals an unprecedented intra-barrel cleavage mechanism and suggests that two conformational changes occur in the beta-domain after cleavage, one conferring increased stability on the beta-domain and another restricting access to the barrel pore." @default.
• W1991736406 created "2016-06-24" @default.
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• W1991736406 date "2007-11-11" @default.
• W1991736406 modified "2023-10-17" @default.
• W1991736406 title "Autotransporter structure reveals intra-barrel cleavage followed by conformational changes" @default.
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• W1991736406 doi "https://doi.org/10.1038/nsmb1322" @default.
• W1991736406 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2551741" @default.
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