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Results 1 - 6 of 6
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217evolution Bacillus subtilis TrmK belongs to the COG2384 (cluster of orthologous groups). The members of this family are found in Gram-negative and Gram-positive bacteria. Their sequences are well-conserved in many bacterial pathogens -, 756149
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217evolution the m1A22 MTase (TrmK) belongs to the COG2384 protein family, RFM/class I, and has orthologues in Gram-positive and Gram-negative bacteria, with no homologues identified in eukaryotes to date. TrmK is well conserved in the bacterial kingdom with enzymes from a number of pathogenic bacteria, e.g. Vibrio cholerae, Listeria monocytogenes, Staphylococcus aureus, Streptococcus pneumoniae, showing a high sequence identity (>40%). The m1A22 modification has been identified only in tRNAs from bacteria -, 756160
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217metabolism the methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding -, 756160
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217more NMR chemical shift mapping is used to get insight on the protein-RNA recognition mode -, 756149
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217more the crystal structure of BsTrmK shows an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. Docking of BstRNASer to BsTrmK in complex with its methyldonor cofactor S-adenosyl-L-methionine (SAM) by NMR chemical shift mapping, modelling, overview. Both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group. BsTrmK requires the intact three-dimensional structure of tRNA to catalyse m1A22 formation -, 757861
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.217physiological function the enzyme is essential for the bacterial survival -, 756160
Results 1 - 6 of 6