期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 18, 期 2, 页码 185-U246出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1981
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资金
- Biotechnology and Biological Sciences Research Council (UK)
- Wellcome Trust (UK)
- Royal Society of New Zealand
- UCB Ltd.
- Commonwealth Scholarships Commission (UK)
- BBSRC [BB/H002677/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H002677/1] Funding Source: researchfish
The >= 10(30) bacteriophages on Earth relentlessly drive adaptive coevolution, forcing the generation of protective mechanisms in their bacterial hosts. One such bacterial phage-resistance system, ToxIN, consists of a protein toxin (ToxN) that is inhibited in vivo by a specific RNA antitoxin (ToxI); however, the mechanisms for this toxicity and inhibition have not been defined. Here we present the crystal structure of the ToxN-ToxI complex from Pectobacterium atrosepticum, determined to 2.75-angstrom resolution. ToxI is a 36-nucleotide noncoding RNA pseudoknot, and three ToxI monomers bind to three ToxN monomers to generate a trimeric ToxN-ToxI complex. Assembly of this complex is mediated entirely through extensive RNA-protein interactions. Furthermore, a 2'-3' cyclic phosphate at the 3' end of ToxI, and catalytic residues, identify ToxN as an endoRNase that processes ToxI from a repetitive precursor but is regulated by its own catalytic product.
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