PDBsum entry 1h6u

Cell adhesion

PDB id: 1h6u

Contents

Protein chain

308 a.a. *

Waters ×403

* Residue conservation analysis

PDB id:

1h6u

Name:

Cell adhesion

Title:

Internalin h: crystal structure of fused n-terminal domains.

Structure:

Internalin h. Chain: a. Fragment: lrr domain, residues 36-343. Engineered: yes

Source:

Listeria monocytogenes. Organism_taxid: 1639. Strain: egd (serovar 1/2a). Expressed in: escherichia coli. Expression_system_taxid: 511693.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.80Å R-factor: 0.170 R-free: 0.217

Authors:

W.-D.Schubert,G.Gobel,M.Diepholz,A.Darji,D.Kloer,T.Hain, T.Chakraborty,J.Wehland,E.Domann,D.W.Heinz

Key ref:

W.D.Schubert et al. (2001). Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. J Mol Biol, 312, 783-794. PubMed id: 11575932 DOI: 10.1006/jmbi.2001.4989

Date:

25-Jun-01 Release date: 11-Oct-01

Protein chain

Q9ZEY1  (Q9ZEY1_LISMN) -  Class 1 internalin InlH from Listeria monocytogenes

Seq: 548 a.a.

Struc: 308 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1006/jmbi.2001.4989

J Mol Biol 312:783-794 (2001)

PubMed id: 11575932

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

W.D.Schubert, G.Göbel, M.Diepholz, A.Darji, D.Kloer, T.Hain, T.Chakraborty, J.Wehland, E.Domann, D.W.Heinz.

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.

Selected figure(s)

Figure 4.
Figure 4. Structure of a single LRR comprising 22 residues. b-Strand and 3[10]-helix are indicated in red and blue, respectively. Side-chain bonds of hydrophobic core residues are shown and labeled in yellow. Exposed residue bonds are shaded gray, while conserved and variable residue positions are labeled in red and black, respectively.[55]

Figure 8.
Figure 8. The continuous hydrophobic core of the internalin domain in InlH[36-343]. The sub-domain colors correspond to Figure 1. The molecular surface is cut away to reveal the interior of the molecule. Hydrophobic amino acid side-chain atoms in the core are shown in yellow. [57]

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 312, 783-794) copyright 2001.

Figures were selected by an automated process.