2B3T

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

2B3T の概要

• エントリーDOI: 10.2210/pdb2b3t/pdb
• 関連するPDBエントリー: 1GQE 1ML5 1NV8 1T43
• 分子名称: Protein methyltransferase hemK, Peptide chain release factor 1, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: release factor; translation termination; methylation; conformational changes, translation
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P0A7I0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71821.48

構造登録者

Graille, M.,Heurgue-Hamard, V.,Champ, S.,Mora, L.,Scrima, N.,Ulryck, N.,van Tilbeurgh, H.,Buckingham, R.H. (登録日: 2005-09-21, 公開日: 2006-01-24, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.1 Å)