Multiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA Methyltransferase

Journal Article · Tue Jan 01 04:00:00 EST 2008 · Structure

DOI:https://doi.org/10.1016/j.str.2008.03.016· OSTI ID:959998

Demirci, H; Gregory, S; Dahlberg, A; Jogl, G

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 a-amino group and the -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 a-amino group in the active site in a trimethylated postcatalytic 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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 959998
• Report Number(s): BNL--82984-2009-JA
• Journal Information: Structure, Journal Name: Structure Journal Issue: 7 Vol. 16
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
ELONGATION
ESCHERICHIA COLI
FLEXIBILITY
LYSINE
ORIENTATION
PROTEINS
SUBSTRATES
SYNTHESIS
national synchrotron light source