Structural highlights
Function[MIAA_ECOLI] Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).[1] [2] 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 PubMedtRNAs that read codons starting with U are usually modified at their A37 by isopentenyl-tRNA transferases in order to minimize peptidyl-tRNA slippage in translation. The consensus substrate requirements of E. coli's isopentenyl-tRNA transferase, MiaA, have been the focus of extensive study. However, the molecular basis of tRNA-MiaA recognition remains unknown. Here, we describe the 2.5 A crystal structure of MiaA in complex with substrate tRNA(Phe). Comparative structural analysis reveals that the enzymatic reaction involves an RNA-protein mutually induced fit mechanism in which large domain movements in MiaA provoke the partial unfolding of the substrate tRNA anticodon loop. In addition, we show how substrate tRNAs are recognized by MiaA through a combination of direct and indirect sequence readouts. RNA-protein mutually induced Fit: Structure of E. coli isopentenyl-tRNA transferase in complex with tRNA(Phe).,Seif E, Hallberg BM J Biol Chem. 2009 Jan 21. PMID:19158097[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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