2FMT

METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET

Summary for 2FMT

• Entry DOI: 10.2210/pdb2fmt/pdb
• Descriptor: FORMYL-METHIONYL-TRNAFMET2, METHIONYL-TRNA FMET FORMYLTRANSFERASE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: complex (methyltransferase-trna), formyltransferase, initiation of translation, complex (methyltransferase-trna) complex, complex (methyltransferase/trna)
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 118211.22

Authors

Schmitt, E.,Mechulam, Y.,Blanquet, S. (deposition date: 1998-07-29, release date: 1999-07-29, Last modification date: 2023-08-02)

Primary citation

Schmitt, E.,Panvert, M.,Blanquet, S.,Mechulam, Y.
Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
EMBO J., 17:6819-6826, 1998

PubMed Abstract: The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet 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.

PubMed: 9843487
DOI: 10.1093/emboj/17.23.6819

Experimental method

X-RAY DIFFRACTION (2.8 Å)