4q2u | pdb_00004q2u

Crystal structure of the E. coli DinJ-YafQ toxin-antitoxin complex

spinqualitylabelsall models 4q2u, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q2u is a 16 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DINJ_ECOLI] Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that counteracts the effect of the YafQ toxin. YafQ and DinJ together bind their own promoter, and by analogy to other TA modules probably repress its expression. Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation. [YAFQ_ECOLI] Toxic component of a toxin-antitoxin (TA) module. A sequence-specific mRNA endoribonuclease that inhibits translation elongation and induces bacterial stasis. Cleavage occurs between the second and third residue of the Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame dependent and occurs within the 5' end of most mRNAs. Ribosome-binding confers the sequence specificity and reading frame-dependence. When overexpressed in liquid media YafQ partially inhibits protein synthesis, with a reduction in growth rate and colony growth rate. This effect is counteracted by coexpression with DinJ, the YafQ antitoxin. YafQ and DinJ together bind their own promoter, and by analogy to other TA modules probably repress its expression. Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation. Publication Abstract from PubMed Bacteria encounter environmental stresses that regulate a gene expression program required for adaptation and survival. Here, we report the 1.8 Angstrom crystal structure of the E. coli toxin-antitoxin complex YafQ-(DinJ)2-YafQ, a key component of the stress response. The antitoxin DinJ dimer adopts a ribbon-helix-helix motif required for transcriptional autorepression while toxin YafQ contains a microbial RNase fold whose proposed active site is concealed by DinJ binding. Contrary to previous reports, our studies indicate that equivalent levels of transcriptional repression occur by direct interaction of either YafQ-(DinJ)2-YafQ or a DinJ dimer at a single inverted repeat of its recognition sequence which overlaps with the -10 promoter region. Surprisingly multiple YafQ-(DinJ)2-YafQ complexes binding to the operator region do not appear to amplify the extent of repression. Our results suggest an alternative model for transcriptional autorepression that may be novel to DinJ-YafQ. Mechanisms of Toxin Inhibition and Transcriptional Repression by E. coli DinJ-YafQ.,Ruangprasert A, Maehigashi T, Miles SJ, Giridharan N, Liu JX, Dunham CM J Biol Chem. 2014 Jun 4. pii: jbc.M114.573006. PMID:24898247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA