1Q82

Crystal Structure of CC-Puromycin bound to the A-site of the 50S ribosomal subunit

1Q82 の概要

• エントリーDOI: 10.2210/pdb1q82/pdb
• 関連するPDBエントリー: 1Q7Y 1Q81 1Q86
• 分子名称: 23S ribosomal rna, Acidic ribosomal protein P0 homolog, L10 Ribosomal Protein, ... (38 entities in total)
• 機能のキーワード: ribosome 50s, puromycin, a-site, protein-protein complex, rna-rna complex, protein-rna complex, ribosome
• 由来する生物種: Haloarcula marismortui; 詳細
• 細胞内の位置: Cytoplasm : P12743
• タンパク質・核酸の鎖数: 31
• 化学式量合計: 1459272.09

構造登録者

Hansen, J.L.,Schmeing, T.M.,Moore, P.B.,Steitz, T.A. (登録日: 2003-08-20, 公開日: 2003-10-07, 最終更新日: 2023-08-16)

主引用文献

Hansen, J.L.,Schmeing, T.M.,Moore, P.B.,Steitz, T.A.
Structural Insights Into Peptide Bond Formation
Proc.Natl.Acad.Sci.USA, 99:11670-11675, 2002

PubMed Abstract: The large ribosomal subunit catalyzes peptide bond formation and will do so by using small aminoacyl- and peptidyl-RNA fragments of tRNA. We have refined at 3-A resolution the structures of both A and P site substrate and product analogues, as well as an intermediate analogue, bound to the Haloarcula marismortui 50S ribosomal subunit. A P site substrate, CCA-Phe-caproic acid-biotin, binds equally to both sites, but in the presence of sparsomycin binds only to the P site. The CCA portions of these analogues are bound identically by either the A or P loop of the 23S rRNA. Combining the separate P and A site substrate complexes into one model reveals interactions that may occur when both are present simultaneously. The alpha-NH(2) group of an aminoacylated fragment in the A site forms one hydrogen bond with the N3 of A2486 (2451) and may form a second hydrogen bond either with the 2' OH of the A-76 ribose in the P site or with the 2' OH of A2486 (2451). These interactions position the alpha amino group adjacent to the carbonyl carbon of esterified P site substrate in an orientation suitable for a nucleophilic attack.

PubMed: 12185246
DOI: 10.1073/pnas.172404099

実験手法

X-RAY DIFFRACTION (2.98 Å)