IPR042221
Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal
InterPro entry
Short name | Leu/Phe-tRNA_Trfase_N |
Overlapping entries |
Description
This superfamily represents the N-terminal domain of leucyl/phenylalanyl-tRNA-protein transferases (L/F-transferases).
L/F-transferase is an N-end rule pathway enzyme, involved in the transfer of Leu and Phe from aminoacyl-tRNAs to exposed N-terminal Arg or Lys residues of acceptor proteins
[1]. This C-terminal domain has a highly conserved fold, observed in the GCN5-related N-acetyltransferase (GNAT) family.
The interface of the N-terminal and C-terminal domains forms a large central cavity, with the characteristic positive charge contributed by the corner of the cleft on the C-terminal domain surface, suggesting that they probably complement the negatively charged phosphate backbone of the substrate aminoacyl-tRNA
[2].
References
1.Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Watanabe K, Toh Y, Suto K, Shimizu Y, Oka N, Wada T, Tomita K. Nature 449, 867-71, (2007). View articlePMID: 17891155
2.The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli. Dong X, Kato-Murayama M, Muramatsu T, Mori H, Shirouzu M, Bessho Y, Yokoyama S. Protein Sci. 16, 528-34, (2007). View articlePMID: 17242373
Cross References
ENZYME
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.30.70.3550