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2.3.2.6: lysine/arginine leucyltransferase

This is an abbreviated version!
For detailed information about lysine/arginine leucyltransferase, go to the full flat file.

Word Map on EC 2.3.2.6

Reaction

L-leucyl-tRNALeu
+
N-terminal L-arginyl-[protein]
=
tRNALeu
+
N-terminal L-leucyl-L-arginyl-[protein]

Synonyms

AAT, aminoacyl transferase, aminoacyl tRNA protein transferase, L/F transferase, L/F-transferase, L/F-tRNA-protein transferase, leucyl, phenylalanine-tRNA-protein transferase, leucyl, phenylalanyl transfer ribonucleic acid-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase, leucyl-phenylalanine-transfer ribonucleate-protein transferase, leucyl/phenylalaninyl tRNA protein transferase, leucyl/phenylalanyl tRNA protein transferase, leucyl/phenylalanyl-tRNA protein transferase, leucyl/phenylalanyl-tRNA-protein transferase, leucyltransferase, LF-transferase, LFTR, R/K-transferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.6 lysine/arginine leucyltransferase

Crystallization

Crystallization on EC 2.3.2.6 - lysine/arginine leucyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.6 A resolution crystal structure
crystal structures of the Escherichia coli LF-transferase complex with phenyalanyl adenosine (rA-Phe), with or without a short peptide bearing an N-terminal Arg residue. In the presence of both the donor and acceptor substrates, the peptide formation proceedes within the crystals, and the product peptide bearing Phe at the N terminus is retained on the LF-transferase
enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX
in complex with minimal substrate phenylalanyl adenosine inhibitor puromycin
-
in complex with puromycin. The p-methoxybenzyl group of puromycin is accomodated in a highly hydrophobic pocket. Model of complex with tRNA and a substrate bearing an N-terminal Arg or Lys