6e8i | pdb_00006e8i

Legionella Longbeachae LeSH (Llo2327) bound to phosphotyrosine

spinqualitylabelsall models 6e8i, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e8i is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PTR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). Apart from a few isolated cases in viruses, no functional SH2 domain has been identified to date in prokaryotes. Here we identify 93 SH2 domains from Legionella that are distinct in sequence and specificity from mammalian SH2 domains. The bacterial SH2 domains are not only capable of binding proteins or peptides in a Tyr phosphorylation-dependent manner, some bind pTyr itself with micromolar affinities, a property not observed for mammalian SH2 domains. The Legionella SH2 domains feature the SH2 fold and a pTyr-binding pocket, but lack a specificity pocket found in a typical mammalian SH2 domain for recognition of sequences flanking the pTyr residue. Our work expands the boundary of phosphotyrosine signalling to prokaryotes, suggesting that some bacterial effector proteins have acquired pTyr-superbinding characteristics to facilitate bacterium-host interactions. Identification and characterization of a large family of superbinding bacterial SH2 domains.,Kaneko T, Stogios PJ, Ruan X, Voss C, Evdokimova E, Skarina T, Chung A, Liu X, Li L, Savchenko A, Ensminger AW, Li SS Nat Commun. 2018 Oct 31;9(1):4549. doi: 10.1038/s41467-018-06943-2. PMID:30382091 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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