4Q2U

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

Summary for 4Q2U

• Entry DOI: 10.2210/pdb4q2u/pdb
• Descriptor: Antitoxin DinJ, mRNA interferase YafQ, SULFATE ION, ... (4 entities in total)
• Functional Keywords: bacterial toxin-antitoxin complex, translation control, rhh motif, ribonuclease, dna binding, ribosome binding, toxin-toxin repressor complex, toxin/toxin repressor
• Biological source: Escherichia coli; More
• Total number of polymer chains: 16
• Total formula weight: 178580.53

Authors

Maehigashi, T.,Ruangprasert, A.,Dunham, C.M. (deposition date: 2014-04-09, release date: 2014-06-11, Last modification date: 2024-11-06)

Primary citation

Ruangprasert, A.,Maehigashi, T.,Miles, S.J.,Giridharan, N.,Liu, J.X.,Dunham, C.M.
Mechanisms of Toxin Inhibition and Transcriptional Repression by Escherichia coli DinJ-YafQ.
J.Biol.Chem., 289:20559-20569, 2014

PubMed Abstract: Bacteria encounter environmental stresses that regulate a gene expression program required for adaptation and survival. Here, we report the 1.8-Å crystal structure of the Escherichia 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, and 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 that 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.

PubMed: 24898247
DOI: 10.1074/jbc.M114.573006

Experimental method

X-RAY DIFFRACTION (1.8 Å)