2c06

NMR-BASED MODEL OF THE COMPLEX OF THE TOXIN KID AND A 5-NUCLEOTIDE SUBSTRATE RNA FRAGMENT (AUACA)

spinqualitylabelsall models 2c06, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c06 is a 3 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1m1f Resources: FirstGlance, OCA, RCSB, PDBsum Function [PEMK_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Probably functions as an mRNA interferase. Responsible for the stable maintenance of the plasmid during cell division by postsegregational killing of plasmid-less daughter cells. Both pemI and PemK proteins bind to the promoter region of the pem operon to autoregulate their synthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The toxin Kid and antitoxin Kis are encoded by the parD operon of Escherichia coli plasmid R1. Kid and its chromosomal homologues MazF and ChpBK have been shown to inhibit protein synthesis in cell extracts and to act as ribosome-independent endoribonucleases in vitro. Kid cleaves RNA preferentially at the 5' side of the A residue in the nucleotide sequence 5'-UA(A/C)-3' of single-stranded regions. Here, we show that RNA cleavage by Kid yields two fragments with a 2':3'-cyclic phosphate group and a free 5'-OH group, respectively. The cleavage mechanism is similar to that of RNases A and T1, involving the uracil 2'-OH group. Via NMR titration studies with an uncleavable RNA mimic, we demonstrate that residues of both monomers of the Kid dimer together form a concatenated RNA-binding surface. Docking calculations based on the NMR chemical shifts, the cleavage mechanism and previously reported mutagenesis data provide a detailed picture of the position of the AUACA fragment within the binding pocket. We propose that residues D75, R73 and H17 form the active site of the Kid toxin, where D75 and R73 are the catalytic base and acid, respectively. The RNA sequence specificity is defined by residues T46, S47, A55, F57, T69, V71 and R73. Our data show the importance of these residues for Kid function, and the implications of our results for related toxins, such as MazF, CcdB and RelE, are discussed. Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system.,Kamphuis MB, Bonvin AM, Monti MC, Lemonnier M, Munoz-Gomez A, van den Heuvel RH, Diaz-Orejas R, Boelens R J Mol Biol. 2006 Mar 17;357(1):115-26. Epub 2005 Dec 27. PMID:16413033 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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