Journal article

Publication year: 2001

Pages: 783-794

Journal: Journal of Molecular Biology

Volume number: 312

Issue number: 4

ISSN: 0022-2836

eISSN: 1089-8638

DOI Link: https://doi.org/10.1006/jmbi.2001.4989

Publisher: Elsevier

Abstract: 
Listeria monocytogenes is an opportunistic, food-borne human and animal pathogen. Host cell invasion requires the action of the internalins A (In1A) and B (In1B), which are members of a family of listerial cell-surface proteins. Common to these proteins are three distinctive N-terminal domains that have been shown to direct host cell-specific invasion for In1A and In1B. Here, we present the high-resolution crystal structures of these domains present in In1B and In1H, and show thai they constitute a single "internalin domain". In this internalin domain, a central LRR region is flanked contiguously by a truncated EF-hand-like cap and an immunoglobulin (1g)-like fold. Tl e extended P-sheet, resulting from the distinctive fusion of the LRR and the Ig-like folds, constitutes an adaptable concave interaction surface, which we propose is responsible for the specific recognition of the host cellular binding partners during infection. (C) 2001 Academic Press.

Harvard Citation style: Schubert, W., Göbel, G., Diepholz, M., Darji, A., Kloer, D., Hain, T., et al. (2001) Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain, Journal of Molecular Biology, 312(4), pp. 783-794. https://doi.org/10.1006/jmbi.2001.4989

APA Citation style: Schubert, W., Göbel, G., Diepholz, M., Darji, A., Kloer, D., Hain, T., Chakraborty, T., Wehland, J., Domann, E., & Heinz, D. (2001). Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. Journal of Molecular Biology. 312(4), 783-794. https://doi.org/10.1006/jmbi.2001.4989