Abstract:
:The ≥ 10³⁰ 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-Å 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.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Blower TR,Pei XY,Short FL,Fineran PC,Humphreys DP,Luisi BF,Salmond GPdoi
10.1038/nsmb.1981subject
Has Abstractpub_date
2011-02-01 00:00:00pages
185-90issue
2eissn
1545-9993issn
1545-9985pii
nsmb.1981journal_volume
18pub_type
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journal_title:Nature structural & molecular biology
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更新日期:2016-06-01 00:00:00
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pub_type: 杂志文章
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