6cp8

Contact-dependent growth inhibition toxin-immunity protein complex from from E. coli 3006

spinqualitylabelsall models 6cp8, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cp8 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.201Å Ligands: EPE, GOL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2A2CAY5_ECOLX Publication Abstract from PubMed Contact-dependent growth inhibition (CDI) is a form of interbacterial competition mediated by CdiB-CdiA two-partner secretion systems. CdiA effector proteins carry polymorphic C-terminal toxin domains (CdiA-CT), which are neutralized by specific CdiI immunity proteins to prevent self-inhibition. Here, we present the crystal structures of CdiA-CTCdiI complexes from Klebsiella pneumoniae 342 and Escherichia coli 3006. The toxins adopt related folds that resemble the ribonuclease domain of colicin D, and both are isoacceptor-specific tRNases that cleave the acceptor stem of deacylated tRNAGAU(Ile). Although the toxins are similar in structure and substrate specificity, CdiA-CT(Kp342) activity requires translation factors EF-Tu and EF-Ts, whereas CdiA-CT(EC3006) is intrinsically active. Furthermore, the corresponding immunity proteins are unrelated in sequence and structure. CdiI(Kp342) forms a dimeric beta sandwich, whereas CdiI(EC3006) is an alpha-solenoid monomer. Given that toxin-immunity genes co-evolve as linked pairs, these observations suggest that the similarities in toxin structure and activity reflect functional convergence. Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.,Gucinski GC, Michalska K, Garza-Sanchez F, Eschenfeldt WH, Stols L, Nguyen JY, Goulding CW, Joachimiak A, Hayes CS Structure. 2019 Sep 6. pii: S0969-2126(19)30281-3. doi:, 10.1016/j.str.2019.08.010. PMID:31515004 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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