Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain

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...

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Bibliographic Details
Published in:Journal of molecular biology 2001-09, Vol.312 (4), p.783-794
Main Authors: Schubert, W D, Göbel, G, Diepholz, M, Darji, A, Kloer, D, Hain, T, Chakraborty, T, Wehland, J, Domann, E, Heinz, D W
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Crystallography, X-Ray
EF Hand Motifs
Humans
Immunoglobulins - chemistry
InlB protein
InlH protein
internalins
Leucine - metabolism
Listeria monocytogenes
Listeria monocytogenes - chemistry
Listeria monocytogenes - genetics
Listeria monocytogenes - pathogenicity
Listeria monocytogenes - physiology
Listeriosis - microbiology
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mice
Mice, Inbred BALB C
Models, Biological
Models, Molecular
Molecular Sequence Data
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Repetitive Sequences, Amino Acid
Sequence Alignment
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.2001.4989