1kqs

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spinqualitylabelsall models 1kqs, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1KQS is a Protein complex structure of sequences from Haloarcula marismortui with MG, K, NA, CD, CL, PPU, PHA, ACA and BTN as ligands. Full crystallographic information is available from OCA.

Reference

A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits., Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA, Nat Struct Biol. 2002 Mar;9(3):225-30. PMID:11828326

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