title: Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
abstract: Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.
authors.affiliation: Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.
authors.forename: Hasan
authors.initials: H
authors.lastname: Demirci
authors.forename: Steven T
authors.initials: ST
authors.lastname: Gregory
authors.forename: Albert E
authors.initials: AE
authors.lastname: Dahlberg
authors.forename: Gerwald
authors.initials: G
authors.lastname: Jogl
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D008745:Methylation; D008958:Models, Molecular; D011487:Protein Conformation; D011496:Protein Methyltransferases / Q000737:chemistry*; D012269:Ribosomal Proteins / Q000737:chemistry*; D012435:S-Adenosylhomocysteine / Q000737:chemistry; D016963:Thermus thermophilus / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; D012435:S-Adenosylhomocysteine; D011496:Protein Methyltransferases