1h6t
From Proteopedia
INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.
Overview
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.
About this Structure
1H6T is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain., Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW, J Mol Biol. 2001 Sep 28;312(4):783-94. PMID:11575932 Page seeded by OCA on Fri May 2 18:30:29 2008
