PDBsum entry 2wqu

Cell invasion

PDB id: 2wqu

Contents

Protein chains

285 a.a. *

264 a.a. *

Ligands

SO4 ×17

GOL ×3

Waters ×61

* Residue conservation analysis

PDB id:

2wqu

Name:

Cell invasion

Title:

Internalin domain of listeria monocytogenes inlb: triclinic crystal form

Structure:

Internalin b. Chain: a, b, c, d, e, f. Fragment: internalin domain, residues 36-321. Engineered: yes

Source:

Listeria monocytogenes. Organism_taxid: 169963. Strain: egd-e. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codonplus.

Resolution:

2.60Å R-factor: 0.194 R-free: 0.249

Authors:

H.H.Niemann,D.W.Heinz

Key ref:

D.M.Ferraris et al. (2010). Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB. J Mol Biol, 395, 522-532. PubMed id: 19900460

Date:

27-Aug-09 Release date: 10-Nov-09

Protein chains

P0DQD2  (INLB_LISMO) -  Internalin B from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

Seq: 630 a.a.

Struc: 285 a.a.

Protein chain

P0DQD2  (INLB_LISMO) -  Internalin B from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

Seq: 630 a.a.

Struc: 264 a.a.

J Mol Biol 395:522-532 (2010)

PubMed id: 19900460

Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB.

D.M.Ferraris, E.Gherardi, Y.Di, D.W.Heinz, H.H.Niemann.

ABSTRACT

The Listeria monocytogenes surface protein InlB mediates bacterial invasion into host cells by activating the human receptor tyrosine kinase Met. So far, it is unknown how InlB or the physiological Met ligand hepatocyte growth factor/scatter factor causes Met dimerization, which is considered a prerequisite for receptor activation. We determined two new structures of InlB, revealing a recurring, antiparallel, dimeric arrangement, in which the two protomers interact through the convex face of the leucine-rich repeat domain. The same contact is found in one structure of the InlB-Met complex. Mutations disrupting the interprotomeric contact of InlB reduced its ability to activate Met and downstream signaling. Conversely, stabilization of this crystal contact by two intermolecular disulfide bonds generates a constitutively dimeric InlB variant with exceptionally high signaling activity, which can stimulate cell motility and cell division. These data demonstrate that the signaling-competent InlB-Met complex assembles with 2:2 stoichiometry around a back-to-back InlB dimer, enabling the direct contact between the stalk region of two Met molecules.