PDBsum entry 2wqx

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protein Protein-protein interface(s) links
Cell invasion PDB id
Jmol PyMol
Protein chains
286 a.a. *
Waters ×369
* Residue conservation analysis
PDB id:
Name: Cell invasion
Title: Inlb321_4r: s199r, d200r, g206r, a227r, c242a mutant of the listeria monocytogenes inlb internalin domain
Structure: Internalin b. Chain: a, b. Fragment: internalin domain, residues 36-321. Synonym: inlb. Engineered: yes. Mutation: yes. Other_details: residues 36-321 of listeria monocytogenes in mutant
Source: Listeria monocytogenes. Organism_taxid: 169963. Strain: egd-e. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codonplus.
2.03Å     R-factor:   0.197     R-free:   0.256
Authors: H.H.Niemann,D.M.Ferraris,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
27-Aug-09     Release date:   10-Nov-09    
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Protein chains
Pfam   ArchSchema ?
P25147  (INLB_LISMO) -  Internalin B
630 a.a.
286 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)


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.
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.