2b3t
From Proteopedia
Structure of complex between E. coli translation termination factor RF1 and the PrmC methyltransferase
Structural highlights
Function[PRMC_ECOLI] Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif, i.e. on 'Gln-235' in RF1 and on 'Gln-252' in RF2.[1] [2] [3] [RF1_ECOLI] Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.[HAMAP-Rule:MF_00093] 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 PubMedClass 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. Molecular basis for bacterial class I release factor methylation by PrmC.,Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH Mol Cell. 2005 Dec 22;20(6):917-27. PMID:16364916[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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