5xun

Crystal structure of Y145F mutant of KacT

spinqualitylabelsall models 5xun, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xun is a 2 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACO, ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A6THQ8_KLEP7 Publication Abstract from PubMed A type II toxin-antitoxin (TA) system, in which the toxin contains a Gcn5-related N-acetyltransferase (GNAT) domain, has been characterized recently. GNAT toxin acetylates aminoacyl-tRNA and blocks protein translation. It is abolished by the cognate antitoxin that contains the ribbon-helix-helix (RHH) domain. Here, we present an experimental demonstration of the interaction of the GNAT-RHH complex with TA promoter DNA. First, the GNAT-RHH TA locus kacAT was found in Klebsiella pneumoniae HS11286, a strain resistant to multiple antibiotics. Overexpression of KacT halted cell growth and resulted in persister cell formation. The crystal structure also indicated that KacT is a typical acetyltransferase toxin. Co-expression of KacA neutralized KacT toxicity. Expression of the bicistronic kacAT locus was up-regulated during antibiotic stress. Finally, KacT and KacA formed a heterohexamer that interacted with promoter DNA, resulting in negative autoregulation of kacAT transcription. The N-terminus region of KacA accounted for specific binding to the palindromic sequence on the operator DNA, whereas its C-terminus region was essential for the inactivation of the GNAT toxin. These results provide an important insight into the regulation of the GNAT-RHH family TA system. Identification and characterization of acetyltransferase-type toxin-antitoxin locus in Klebsiella pneumoniae.,Qian H, Yao Q, Tai C, Deng Z, Gan J, Ou HY Mol Microbiol. 2018 May;108(4):336-349. doi: 10.1111/mmi.13934. Epub 2018 Mar 8. PMID:29461656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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