2CXA

Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli

Summary for 2CXA

• Entry DOI: 10.2210/pdb2cxa/pdb
• Descriptor: Leucyl/phenylalanyl-tRNA-protein transferase (2 entities in total)
• Functional Keywords: transferase, aminoacyl-trna, protein degradation, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8P1
• Total number of polymer chains: 1
• Total formula weight: 29548.37

Authors

Kato-Murayama, M.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-06-28, release date: 2005-12-28, Last modification date: 2024-10-30)

Primary citation

Dong, X.,Kato-Murayama, M.,Muramatsu, T.,Mori, H.,Shirouzu, M.,Bessho, Y.,Yokoyama, S.
The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli
Protein Sci., 16:528-534, 2007

PubMed Abstract: Leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) is an N-end rule pathway enzyme, which catalyzes the transfer of Leu and Phe from aminoacyl-tRNAs to exposed N-terminal Arg or Lys residues of acceptor proteins. Here, we report the 1.6 A resolution crystal structure of L/F-transferase (JW0868) from Escherichia coli, the first three-dimensional structure of an L/F-transferase. The L/F-transferase adopts a monomeric structure consisting of two domains that form a bilobate molecule. The N-terminal domain forms a small lobe with a novel fold. The large C-terminal domain has a highly conserved fold, which is observed in the GCN5-related N-acetyltransferase (GNAT) family. Most of the conserved residues of L/F-transferase reside in the central cavity, which exists at the interface between the N-terminal and C-terminal domains. A comparison of the structures of L/F-transferase and the bacterial peptidoglycan synthase FemX, indicated a structural homology in the C-terminal domain, and a similar domain interface region. Although the peptidyltransferase function is shared between the two proteins, the enzymatic mechanism would differ. The conserved residues in the central cavity of L/F-transferase suggest that this region is important for the enzyme catalysis.

PubMed: 17242373
DOI: 10.1110/ps.062616107

Experimental method

X-RAY DIFFRACTION (1.6 Å)