Ontology highlight
ABSTRACT:
SUBMITTER: Dong X
PROVIDER: S-EPMC2203310 | biostudies-literature | 2007 Mar
REPOSITORIES: biostudies-literature
Dong Xuesong X Kato-Murayama Miyuki M Muramatsu Tomonari T Mori Hirotada H Shirouzu Mikako M Bessho Yoshitaka Y Yokoyama Shigeyuki S
Protein science : a publication of the Protein Society 20070122 3
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. Th ...[more]