2B3T

Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase

Summary for 2B3T

• Entry DOI: 10.2210/pdb2b3t/pdb
• Related: 1GQE 1ML5 1NV8 1T43
• Descriptor: Protein methyltransferase hemK, Peptide chain release factor 1, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: release factor; translation termination; methylation; conformational changes, translation
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A7I0
• Total number of polymer chains: 2
• Total formula weight: 71821.48

Authors

Graille, M.,Heurgue-Hamard, V.,Champ, S.,Mora, L.,Scrima, N.,Ulryck, N.,van Tilbeurgh, H.,Buckingham, R.H. (deposition date: 2005-09-21, release date: 2006-01-24, Last modification date: 2024-02-14)

Primary citation

Graille, M.,Heurgue-Hamard, V.,Champ, S.,Mora, L.,Scrima, N.,Ulryck, N.,van Tilbeurgh, H.,Buckingham, R.H.
Molecular basis for bacterial class I release factor methylation by PrmC
Mol.Cell, 20:917-927, 2005

PubMed Abstract: Class I release factors bind to ribosomes in response to stop codons and trigger peptidyl-tRNA hydrolysis at the P site. Prokaryotic and eukaryotic RFs share one motif: a GGQ tripeptide positioned in a loop at the end of a stem region that interacts with the ribosomal peptidyl transferase center. The glutamine side chain of this motif is specifically methylated in both prokaryotes and eukaryotes. Methylation in E. coli is due to PrmC and results in strong stimulation of peptide chain release. We have solved the crystal structure of the complex between E. coli RF1 and PrmC bound to the methyl donor product AdoHCy. Both the GGQ domain (domain 3) and the central region (domains 2 and 4) of RF1 interact with PrmC. Structural and mutagenic data indicate a compact conformation of RF1 that is unlike its conformation when it is bound to the ribosome but is similar to the crystal structure of the protein alone.

PubMed: 16364916
DOI: 10.1016/j.molcel.2005.10.025

Experimental method

X-RAY DIFFRACTION (3.1 Å)