Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
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.
Demirci
Hasan
H
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.
Gregory
Steven T
ST
Dahlberg
Albert E
AE
Jogl
Gerwald
G
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
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; D012435:S-Adenosylhomocysteine; D011496:Protein Methyltransferases