Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.

ABSTRACT: Bacterial and eukaryotic tRNAs that decode codons starting with uridine have a hydrophobically hypermodified adenosine at position 37 (A(37)) adjacent to the 3'-end of the anticodon, which is essential for efficient and highly accurate protein translation by the ribosome. However, it remains unclear as to how the corresponding tRNAs are selected to be modified by alkylation at the correct position of the adenosine base. We have determined a series of crystal structures of bacterial tRNA isopentenyltransferase (MiaA) in apo- and tRNA-bound forms, which completely render snapshots of substrate selections during the modification of RNA. A compact evolutionary inserted domain (herein swinging domain) in MiaA that exhibits as a highly mobile entity moves around the catalytic domain as likely to

SUBMITTER: Chimnaronk S 

PROVIDER: S-EPMC2786004 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature