Recognition of Ribosomal Protein L11 by the Protein Trimethyltransferase PrmA

Journal Article · Mon Jan 01 04:00:00 EST 2007 · EMBO Journal

DOI:https://doi.org/10.1038/sj.emboj.7601508· OSTI ID:929859

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

Bacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 {angstrom} resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 {angstrom} each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 {angstrom} resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 929859
• Report Number(s): BNL--80425-2008-JA
• Journal Information: EMBO Journal, Journal Name: EMBO Journal Vol. 26; ISSN EMJODG; ISSN 0261-4189
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
BACTERIA
CELL CONSTITUENTS
DISSOCIATION
ENZYMES
INTERACTIONS
METHYLATION
PROTEINS
RESIDUES
SUBSTRATES
national synchrotron light source