PDBsum entry: 1e5u

Intimin

PDB id: 1e5u

Contents

Protein chain

187 a.a. *

* Residue conservation analysis

PDB id:

1e5u

Name:

Intimin

Title:

Nmr representative structure of intimin-190 (int190) from enteropathogenic e. Coli

Structure:

Intimin. Chain: i. Fragment: c-terminal 190 residue-fragment. Synonym: int190. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: enteropathogenic serotype o127\:h6. Variant: strain e2348/69. Cell: bacterial. Cellular_location: outer membrane/surface. Gene: eae. Expressed in: escherichia coli. Expression_system_taxid: 511693.

NMR struc:

1 models

Authors:

S.Prasannan,S.J.Matthews,M.Batchelor,S.Daniell,S.Reece, G.Frankel,G.Dougan,I.Connerton,G.Bloomberg

Key ref:

M.Batchelor et al. (2000). Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli. EMBO J, 19, 2452-2464. PubMed id: 10835344 DOI: 10.1093/emboj/19.11.2452

Date:

02-Aug-00 Release date: 16-Aug-00

Supersedes:

1e1b

Protein chain

P19809  (EAE_ECO27) -  Intimin

Seq: 939 a.a.

Struc: 187 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cell surface (1 term)
• Biological process: pathogenesis (1 term)
• Biochemical function: binding (1 term)

DOI no: 10.1093/emboj/19.11.2452

EMBO J 19:2452-2464 (2000)

PubMed id: 10835344

Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli.

M.Batchelor, S.Prasannan, S.Daniell, S.Reece, I.Connerton, G.Bloomberg, G.Dougan, G.Frankel, S.Matthews.

ABSTRACT

Intimin is a bacterial adhesion molecule involved in intimate attachment of enteropathogenic and enterohaemorrhagic Escherichia coli to mammalian host cells. Intimin targets the translocated intimin receptor (Tir), which is exported by the bacteria and integrated into the host cell plasma membrane. In this study we localized the Tir-binding region of intimin to the C-terminal 190 amino acids (Int190). We have also determined the region's high-resolution solution structure, which comprises an immunoglobulin domain that is intimately coupled to a novel C-type lectin domain. This fragment, which is necessary and sufficient for Tir interaction, defines a new super domain in intimin that exhibits striking structural similarity to the integrin-binding domain of the Yersinia invasin and C-type lectin families. The extracellular portion of intimin comprises an articulated rod of immunoglobulin domains extending from the bacterium surface, conveying a highly accessible 'adhesive tip' to the target cell. The interpretation of NMR-titration and mutagenesis data has enabled us to identify, for the first time, the binding site for Tir, which is located at the extremity of the Int190 moiety.

Selected figure(s)

Figure 1.
Figure 1 Schematic representation of the overlapping Int280-derived polypeptides. The two IgSF-like domains (D2 and D3), the C-type lectin-like domain (D4) and the conserved motifs in Int280 are shown at the top. The position of W150 within Int190 is indicated. Numbers on both sides of the fragments mark the first and last amino acids of each fragment within the Int280 domain.

Figure 3.
Figure 3 (A) C[ ]traces representing the superimposition of the 15 refined Int188 structures. (B) C[ ]traces representing the superimposition of the 15 refined Int188 structures. The orientations of (A) and (B) are related by a 90° rotation. (C) Schematic representation of Int188 for the orientation displayed in (A). (D) Schematic representation of Int188 domains for the orientation displayed in (B). (E) A 'flattened' illustration highlighting the topology of Int188. Helices are represented as open tubes and -strands as arrows.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 2452-2464) copyright 2000.

Figures were selected by the author.