Structural highlights
Function
[PRMA_THET8] Methylates ribosomal protein L11; this reaction probably occurs before the protein is assembled into the ribosome. This function is dispensable for growth and thermostability. [RL11_THETH] This protein binds directly to 23S ribosomal RNA (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.,Demirci H, Gregory ST, Dahlberg AE, Jogl G Structure. 2008 Jul;16(7):1059-66. PMID:18611379[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Demirci H, Gregory ST, Dahlberg AE, Jogl G. Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Structure. 2008 Jul;16(7):1059-66. PMID:18611379 doi:10.1016/j.str.2008.03.016
