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Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.

Structure. 2019;

Gucinski GC, Michalska K, Garza-Sánchez F, Eschenfeldt WH, Stols L, Nguyen JY, Goulding CW, Joachimiak A, Hayes CS.

Products/Services Used	Details	Operation
Custom DNA/RNA Oligos	, 2007) N/A Critical Commercial Assays The Protein Complex Suite Qiagen Deposited Data Structure data and reﬁnement statistics for CdiA-CT,CdiIKp342 complex Structure data and reﬁnement statistics for CdiA-CT,CdiIEC3006 complex This paper PDB: 6CP9 This paper PDB: 6CP8 Oligonucleotides Complete list of oligonucleotides and PCR primers This paper see Table S3 Recombinant DNA pET21b Novagen Cat# 69741-3 pTrc99A Amersham N/A pCH978 This paper N/A pCH6283 Genscript N/A pCH6289 Genscript N/A pCH7171 (Johnson et al....010 Protein Over-production Plasmids The coding sequences for CdiA-CT/CdiIKp342 and CdiA-CT/CdiIEC3006 were synthesized by Genscript (Piscataway, NJ) and supplied in the pUC57 vector (pCH6289 and pCH6283).	Get A Quote

摘要

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-CT⋅CdiI 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 tRNAGAUIle. Although the toxins are similar in structure and substrate specificity, CdiA-CTKp342 activity requires translation... More