4aw4 | pdb_00004aw4

Engineered variant of Listeria monocytogenes InlB internalin domain with an additional leucine rich repeat inserted

spinqualitylabelsall models 4aw4, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aw4 is a 3 chain structure with sequence from Lismo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Related: 1d0b, 1h6t, 1m9s, 1otm, 1otn, 1oto, 2uzx, 2uzy, 2wqu, 2wqv, 2wqw, 2wqx, 2y5p, 2y5q Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [INLB_LISMO] Mediates the entry of Listeria monocytogenes into cells. Publication Abstract from PubMed The physiological relevance of contacts in crystal lattices often remains elusive. This was also the case for the complex between the invasion protein internalin B (InlB) from Listeria monocytogenes and its host cell receptor, the human receptor tyrosine kinase (RTK) MET. InlB is aMET agonist and induces bacterialhost cell invasion.Activation of RTKs generally involves ligand-induced dimerization of the receptor ectodomain. The two currently available crystal structures of the InlB:MET complex show the same arrangement of InlB and MET in a 1:1 complex, but different dimeric 2:2 assemblies. Only one of these 2:2 assemblies is predicted to be stable by a computational procedure. This assembly is mainly stabilized by a contact between the Cap domain of InlB from one and the Sema domain of MET from another 1:1 complex.Here, we probe the physiological relevance of this interaction. We generatedvariants of the leucine-rich repeat (LRR) protein InlBby inserting an additional repeat between the first and the second LRR. This should allow formation of the 1:1 complex but disrupt the potential 2:2 complex involving the Cap-Sema contact due to steric distortions. A crystal structure of oneof the engineered proteins showed that it folded properly. Binding affinityto MET was comparable to that of wild-type InlB. The InlB variant induced MET phosphorylation and cell scatter like wild-type InlB.Theseresults suggestthat the Cap-Sema interaction is not physiologically relevant and support the previously proposed assembly, in which a 2:2 InlB-MET complex is built around a ligand dimer. Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex.,Niemann HH, Gherardi E, Bleymuller WM, Heinz DW Protein Sci. 2012 Aug 10. doi: 10.1002/pro.2142. PMID:22887347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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