1KQS

The Haloarcula marismortui 50S Complexed with a Pretranslocational Intermediate in Protein Synthesis

1KQS の概要

• エントリーDOI: 10.2210/pdb1kqs/pdb
• 関連するPDBエントリー: 1ffk 1ffz 1jj2
• 分子名称: 23S RRNA, RIBOSOMAL PROTEIN L7AE, RIBOSOMAL PROTEIN L10, ... (42 entities in total)
• 機能のキーワード: ribosome assembly, rna-rna, protein-rna, protein-protein, protein synthesis, peptidyl transferase, ribosome
• 由来する生物種: Haloarcula marismortui; 詳細
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 1460691.37

構造登録者

Schmeing, T.M.,Seila, A.C.,Hansen, J.L.,Freeborn, B.,Soukup, J.K.,Scaringe, S.A.,Strobel, S.A.,Moore, P.B.,Steitz, T.A. (登録日: 2002-01-07, 公開日: 2002-02-22, 最終更新日: 2023-11-15)

主引用文献

Schmeing, T.M.,Seila, A.C.,Hansen, J.L.,Freeborn, B.,Soukup, J.K.,Scaringe, S.A.,Strobel, S.A.,Moore, P.B.,Steitz, T.A.
A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits.
Nat.Struct.Biol., 9:225-230, 2002

PubMed Abstract: The large ribosomal subunit catalyzes peptide bond formation during protein synthesis. Its peptidyl transferase activity has often been studied using a 'fragment assay' that depends on high concentrations of methanol or ethanol. Here we describe a version of this assay that does not require alcohol and use it to show, both crystallographically and biochemically, that crystals of the large ribosomal subunits from Haloarcula marismortui are enzymatically active. Addition of these crystals to solutions containing substrates results in formation of products, which ceases when crystals are removed. When substrates are diffused into large subunit crystals, the subsequent structure shows that products have formed. The CC-puromycin-peptide product is found bound to the A-site and the deacylated CCA is bound to the P-site, with its 3prime prime or minute OH near N3 A2486 (Escherichia coli A2451). Thus, this structure represents a state that occurs after peptide bond formation but before the hybrid state of protein synthesis.

PubMed: 11828326

実験手法

X-RAY DIFFRACTION (3.1 Å)