4px8 | pdb_00004px8

Structure of P. vulgaris HigB toxin

spinqualitylabelsall models 4px8, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4px8 is a 1 chain structure with sequence from Proteus vulgaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.25Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HIGB_PROVU Toxic component of a type II toxin-antitoxin (TA) module (PubMed:19423702, PubMed:24257752, PubMed:8645296). A ribosome-associated translation-dependent mRNA interferase. Inhibits translation by sequence-specific cleavage of mRNA. Prefers either in-frame or out-of-frame 5'-AAA-3' codons (lysine). Cleaves also the first three AAAs of stretches of four or more A sequences. 20% of codons containing AA are cleaved and occassionally cuts even at a single A (PubMed:19423702). Publication Abstract from PubMed Bacteria contain multiple type II toxins that selectively degrade mRNAs bound to the ribosome to regulate translation and growth and facilitate survival during the stringent response. Ribosome-dependent toxins recognize a variety of three-nucleotide codons within the aminoacyl (A) site, but how these endonucleases achieve substrate specificity remains poorly understood. Here, we identify the critical features for how the host inhibition of growth B (HigB) toxin recognizes each of the three A-site nucleotides for cleavage. X-ray crystal structures of HigB bound to two different codons on the ribosome illustrate how HigB uses a microbial RNase-like nucleotide recognition loop to recognize either cytosine or adenosine at the second A-site position. Strikingly, a single HigB residue and 16S rRNA residue C1054 form an adenosine-specific pocket at the third A-site nucleotide, in contrast to how tRNAs decode mRNA. Our results demonstrate that the most important determinant for mRNA cleavage by ribosome-dependent toxins is interaction with the third A-site nucleotide. Defining the mRNA recognition signature of a bacterial toxin protein.,Schureck MA, Dunkle JA, Maehigashi T, Miles SJ, Dunham CM Proc Natl Acad Sci U S A. 2015 Nov 10;112(45):13862-7. doi:, 10.1073/pnas.1512959112. Epub 2015 Oct 27. PMID:26508639 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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