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Journal Article

Crystal structure of the autochaperone region from the Shigella flexneri autotransporter IcsA.

MPS-Authors
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Kühnel,  K.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Diezmann,  D.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

External Resource
Fulltext (public)

883595.pdf
(Publisher version), 692KB

Supplementary Material (public)

883595-Suppl.doc
(Supplementary material), 2MB

Citation

Kühnel, K., & Diezmann, D. (2011). Crystal structure of the autochaperone region from the Shigella flexneri autotransporter IcsA. Journal of Bacteriology, 193(8), 2042-2045. doi:10.1128/​JB.00790-10.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0011-561C-2
Abstract
The IcsA (intracellular spread gene A) autotransporter from Shigella flexneri is a key virulence factor. We identified a stable fragment comprising residues 591 to 758, which corresponds to the autochaperone region of the IcsA passenger domain. We showed that thermal unfolding of the autochaperone region is reversible and determined its crystal structure at 2.0-Å resolution.