| Structural highlights
2b3t is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Related: | 1ml5, 1gqe, 1nv8, 1t43 |
| Gene: | hemK ("Bacillus coli" Migula 1895), prfA, sueB, uar ("Bacillus coli" Migula 1895) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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 PubMed
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.
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
- ↑ Nakahigashi K, Kubo N, Narita S, Shimaoka T, Goto S, Oshima T, Mori H, Maeda M, Wada C, Inokuchi H. HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1473-8. Epub 2002 Jan 22. PMID:11805295 doi:http://dx.doi.org/10.1073/pnas.032488499
- ↑ Heurgue-Hamard V, Champ S, Engstrom A, Ehrenberg M, Buckingham RH. The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors. EMBO J. 2002 Feb 15;21(4):769-78. PMID:11847124 doi:http://dx.doi.org/10.1093/emboj/21.4.769
- ↑ Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH. Molecular basis for bacterial class I release factor methylation by PrmC. Mol Cell. 2005 Dec 22;20(6):917-27. PMID:16364916 doi:10.1016/j.molcel.2005.10.025
- ↑ Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH. Molecular basis for bacterial class I release factor methylation by PrmC. Mol Cell. 2005 Dec 22;20(6):917-27. PMID:16364916 doi:10.1016/j.molcel.2005.10.025
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