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PDBsum entry 2wqv

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protein ligands Protein-protein interface(s) links
Cell invasion PDB id
2wqv
Jmol
Contents
Protein chains
280 a.a. *
Ligands
PG4 ×2
PGE ×4
Waters ×31
* Residue conservation analysis
PDB id:
2wqv
Name: Cell invasion
Title: Internalin domain of listeria monocytogenes inlb: rhombohedral crystal form
Structure: Internalin b. Chain: a, b. 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:
2.80Å     R-factor:   0.205     R-free:   0.237
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 DOI: 10.1016/j.jmb.2009.10.074
Date:
27-Aug-09     Release date:   10-Nov-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P25147  (INLB_LISMO) -  Internalin B
Seq:
Struc:
 
Seq:
Struc:
630 a.a.
280 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jmb.2009.10.074 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.