1H6U

Internalin H: crystal structure of fused N-terminal domains.

Summary for 1H6U

• Entry DOI: 10.2210/pdb1h6u/pdb
• Descriptor: INTERNALIN H (2 entities in total)
• Functional Keywords: cell adhesion, leucine rich repeat, ig-like domain, ef-hand domain
• Biological source: LISTERIA MONOCYTOGENES
• Total number of polymer chains: 1
• Total formula weight: 32585.61

Authors

Schubert, W.-D.,Gobel, G.,Diepholz, M.,Darji, A.,Kloer, D.,Hain, T.,Chakraborty, T.,Wehland, J.,Domann, E.,Heinz, D.W. (deposition date: 2001-06-25, release date: 2001-10-11, Last modification date: 2023-12-13)

Primary citation

Schubert, W.D.,Gobel, G.,Diepholz, M.,Darji, A.,Kloer, D.,Hain, T.,Chakraborty, T.,Wehland, J.,Domann, E.,Heinz, D.W.
Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain.
J.Mol.Biol., 312:783-794, 2001

PubMed Abstract: Listeria monocytogenes is an opportunistic, food-borne human and animal pathogen. Host cell invasion requires the action of the internalins A (InlA) and B (InlB), 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 InlA and InlB. Here, we present the high-resolution crystal structures of these domains present in InlB and InlH, and show that 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 (Ig)-like fold. The extended beta-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.

PubMed: 11575932
DOI: 10.1006/jmbi.2001.4989

Experimental method

X-RAY DIFFRACTION (1.8 Å)