2fca
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The structure of BsTrmB
OverviewOverview
The structure of Bacillus subtilis TrmB (BsTrmB), the tRNA (m7G46), methyltransferase, was determined at a resolution of 2.1 A. This is the, first structure of a member of the TrmB family to be determined by X-ray, crystallography. It reveals a unique variant of the Rossmann-fold, methyltransferase (RFM) structure, with the N-terminal helix folded on the, opposite site of the catalytic domain. The architecture of the active site, and a computational docking model of BsTrmB in complex with the methyl, group donor S-adenosyl-L-methionine and the tRNA substrate provide an, explanation for results from mutagenesis studies of an orthologous enzyme, from Escherichia coli (EcTrmB). However, unlike EcTrmB, BsTrmB is shown, here to be dimeric both in the crystal and in solution. The dimer, interface has a hydrophobic core and buries a potassium ion and five water, molecules. The evolutionary analysis of the putative interface residues in, the TrmB family suggests that homodimerization may be a specific feature, of TrmBs from Bacilli, which may represent an early stage of evolution to, an obligatory dimer.
About this StructureAbout this Structure
2FCA is a Single protein structure of sequence from Bacillus subtilis with K as ligand. Active as tRNA (guanine-N(7)-)-methyltransferase, with EC number 2.1.1.33 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase., Zegers I, Gigot D, van Vliet F, Tricot C, Aymerich S, Bujnicki JM, Kosinski J, Droogmans L, Nucleic Acids Res. 2006 Apr 5;34(6):1925-34. Print 2006. PMID:16600901
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