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Crystal structure of methionyl‐tRNA f Met transformylase complexed with the initiator formyl‐methionyl‐tRNA f Met
Author(s) -
Schmitt Emmanuelle,
Panvert Michel,
Blanquet Sylvain,
Mechulam Yves
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.23.6819
Subject(s) - transfer rna , biology , formylation , acceptor , stereochemistry , escherichia coli , biochemistry , enzyme , elongation factor , transferase , rna , chemistry , ribosome , catalysis , gene , physics , condensed matter physics
The crystal structure of Escherichia coli methionyl‐tRNA f Met transformylase complexed with formyl‐methionyl‐tRNA f Met was solved at 2.8 Å resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl‐tRNA f Met to initiation of translation in eubacteria. In the three‐dimensional model, the methionyl‐tRNA f Met formyltransferase fills in the inside of the L‐shaped tRNA molecule on the D‐stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1‐A72 mismatch characteristic of the initiator tRNA is split and the 3′ arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T‐stem side.