1R5O

crystal structure analysis of sup35 complexed with GMPPNP

1R5O の概要

• エントリーDOI: 10.2210/pdb1r5o/pdb
• 関連するPDBエントリー: 1R5B 1R5N
• 分子名称: Eukaryotic peptide chain release factor GTP-binding subunit, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (3 entities in total)
• 機能のキーワード: translation termination, peptide release, gtpase, translation
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• 細胞内の位置: Cytoplasm (Probable): O74718
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52625.39

構造登録者

Kong, C.,Song, H. (登録日: 2003-10-11, 公開日: 2004-05-25, 最終更新日: 2023-10-25)

主引用文献

Kong, C.,Ito, K.,Walsh, M.A.,Wada, M.,Liu, Y.,Kumar, S.,Barford, D.,Nakamura, Y.,Song, H.
Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe
Mol.Cell, 14:233-245, 2004

PubMed Abstract: Translation termination in eukaryotes is governed by two interacting release factors, eRF1 and eRF3. The crystal structure of the eEF1alpha-like region of eRF3 from S. pombe determined in three states (free protein, GDP-, and GTP-bound forms) reveals an overall structure that is similar to EF-Tu, although with quite different domain arrangements. In contrast to EF-Tu, GDP/GTP binding to eRF3c does not induce dramatic conformational changes, and Mg(2+) is not required for GDP binding to eRF3c. Mg(2+) at higher concentration accelerates GDP release, suggesting a novel mechanism for nucleotide exchange on eRF3 from that of other GTPases. Mapping sequence conservation onto the molecular surface, combined with mutagenesis analysis, identified the eRF1 binding region, and revealed an essential function for the C terminus of eRF3. The N-terminal extension, rich in acidic amino acids, blocks the proposed eRF1 binding site, potentially regulating eRF1 binding to eRF3 in a competitive manner.

PubMed: 15099522
DOI: 10.1016/S1097-2765(04)00206-0

実験手法

X-RAY DIFFRACTION (3.2 Å)