1KQS

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

Summary for 1KQS

• Entry DOI: 10.2210/pdb1kqs/pdb
• Related: 1ffk 1ffz 1jj2
• Descriptor: 23S RRNA, RIBOSOMAL PROTEIN L7AE, RIBOSOMAL PROTEIN L10, ... (42 entities in total)
• Functional Keywords: ribosome assembly, rna-rna, protein-rna, protein-protein, protein synthesis, peptidyl transferase, ribosome
• Biological source: Haloarcula marismortui; More
• Total number of polymer chains: 32
• Total formula weight: 1460691.37

Authors

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. (deposition date: 2002-01-07, release date: 2002-02-22, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)