1h6t

From Proteopedia

Revision as of 14:25, 5 November 2007

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. Structure known Active Site: NUL. 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

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