PDBsum entry 2k2s

Cell adhesion

PDB id

2k2s

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Contents

			Protein chains

					136 a.a.


					55 a.a.

PDB id:

2k2s

Links

Name:

Cell adhesion

Title:

Structure of the mic1-gld/mic6-egf complex from toxoplasma gondii

Structure:

Micronemal protein 1. Chain: a. Fragment: galectin-like domain (unp residues 320-455). Engineered: yes. Micronemal protein 6. Chain: b. Fragment: egf-like domain (unp residues 87-147). Engineered: yes

Source:

Toxoplasma gondii. Organism_taxid: 5811. Gene: mic1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: mic6.

NMR struc:

1 models

Authors:

S.Matthews

Key ref:

K.Sawmynaden et al. (2008). Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition. Embo Rep, 9, 1149-1155. PubMed id: 18818666

Date:

11-Apr-08

Release date:

24-Feb-09

PROCHECK

	Headers

	References

Protein chain

O00834 (MIC1_TOXGO) - Micronemal protein 1 from Toxoplasma gondii

Seq: Struc:					456 a.a. 136 a.a.

Protein chain

Q9XYH7 (MIC6_TOXGO) - Micronemal protein 6 from Toxoplasma gondii

Seq: Struc:					349 a.a. 55 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Embo Rep 9:1149-1155 (2008)
PubMed id: 18818666

Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition.
K.Sawmynaden, S.Saouros, N.Friedrich, J.Marchant, P.Simpson, B.Bleijlevens, M.J.Blackman, D.Soldati-Favre, S.Matthews.

ABSTRACT

The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Adhesive complexes composed of microneme proteins (MICs) are secreted onto the parasite surface from intracellular stores and fulfil crucial roles in host-cell recognition, attachment and penetration. Here, we report the high-resolution solution structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore, we identify two analogous interaction sites within separate epidermal growth factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both interactions are functional for the recognition of host cell receptor in the parasite, using immunofluorescence and invasion assays. The nature of this new mode of recognition of the EGF domain and its abundance in apicomplexan surface proteins suggest a more generalized means of constructing functional assemblies by using EGF domains with highly specific receptor-binding properties.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19901027

N.Friedrich, J.M.Santos, Y.Liu, A.S.Palma, E.Leon, S.Saouros, M.Kiso, M.J.Blackman, S.Matthews, T.Feizi, and D.Soldati-Favre (2010).
Members of a novel protein family containing microneme adhesive repeat domains act as sialic acid-binding lectins during host cell invasion by apicomplexan parasites.

J Biol Chem, 285, 2064-2076.

20485485

P.W.Chiu, Y.C.Huang, Y.J.Pan, C.H.Wang, and C.H.Sun (2010).
A novel family of cyst proteins with epidermal growth factor repeats in Giardia lamblia.

PLoS Negl Trop Dis, 4, e677.

19593815

J.A.Garnett, Y.Liu, E.Leon, S.A.Allman, N.Friedrich, S.Saouros, S.Curry, D.Soldati-Favre, B.G.Davis, T.Feizi, and S.Matthews (2009).
Detailed insights from microarray and crystallographic studies into carbohydrate recognition by microneme protein 1 (MIC1) of Toxoplasma gondii.

Protein Sci, 18, 1935-1947.

PDB codes:

3f53 3f5a 3f5e

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.