2LLZ

GhoS (YjdK) monomer

Summary for 2LLZ

• Entry DOI: 10.2210/pdb2llz/pdb
• NMR Information: BMRB: 18086
• Descriptor: Uncharacterized protein yjdK (1 entity in total)
• Functional Keywords: rnase, biofilm, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 11672.12

Authors

Lord, D.,Peti, W.,Page, R. (deposition date: 2011-11-18, release date: 2012-09-05, Last modification date: 2024-05-15)

Primary citation

Wang, X.,Lord, D.M.,Cheng, H.Y.,Osbourne, D.O.,Hong, S.H.,Sanchez-Torres, V.,Quiroga, C.,Zheng, K.,Herrmann, T.,Peti, W.,Benedik, M.J.,Page, R.,Wood, T.K.
A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS.
Nat.Chem.Biol., 8:855-861, 2012

PubMed Abstract: Among bacterial toxin-antitoxin systems, to date no antitoxin has been identified that functions by cleaving toxin mRNA. Here we show that YjdO (renamed GhoT) is a membrane lytic peptide that causes ghost cell formation (lysed cells with damaged membranes) and increases persistence (persister cells are tolerant to antibiotics without undergoing genetic change). GhoT is part of a new toxin-antitoxin system with YjdK (renamed GhoS) because in vitro RNA degradation studies, quantitative real-time reverse-transcription PCR and whole-transcriptome studies revealed that GhoS masks GhoT toxicity by cleaving specifically yjdO (ghoT) mRNA. Alanine substitutions showed that Arg28 is important for GhoS activity, and RNA sequencing indicated that the GhoS cleavage site is rich in U and A. The NMR structure of GhoS indicates it is related to the CRISPR-associated-2 RNase, and GhoS is a monomer. Hence, GhoT-GhoS is to our knowledge the first type V toxin-antitoxin system where a protein antitoxin inhibits the toxin by cleaving specifically its mRNA.

PubMed: 22941047
DOI: 10.1038/nchembio.1062

Experimental method

SOLUTION NMR