1ond
From Proteopedia
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THE CRYSTAL STRUCTURE OF THE 50S LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS COMPLEXED WITH TROLEANDOMYCIN MACROLIDE ANTIBIOTIC
Overview
Nascent proteins emerge out of ribosomes through an exit tunnel, which was, assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in, sequence-specific gating of nascent chains and in responding to cellular, signals. Consistently, modulation of the tunnel shape, caused by the, binding of the semi-synthetic macrolide troleandomycin to the large, ribosomal subunit from Deinococcus radiodurans, was revealed, crystallographically. The results provide insights into the tunnel, dynamics at high resolution. Here we show that, in addition to the typical, steric blockage of the ribosomal tunnel by macrolides, troleandomycin, induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved beta-hairpin across the tunnel., On the basis of mutations that alleviate elongation arrest, the tunnel, motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may, induce a similar gating mechanism.
About this Structure
1OND is a Protein complex structure of sequences from Deinococcus radiodurans with TAO as ligand. Full crystallographic information is available from OCA.
Reference
Structural insight into the role of the ribosomal tunnel in cellular regulation., Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A, Nat Struct Biol. 2003 May;10(5):366-70. PMID:12665853
Page seeded by OCA on Tue Nov 20 23:02:10 2007
Categories: Deinococcus radiodurans | Protein complex | Auerbach, T. | Baram, D. | Bashan, A. | Berisio, R. | Harms, J. | Schluenzen, F. | Yonath, A. | TAO | Antibiotic | Blockage | Exit-tunnel l22 | Macrolide | Ribosomes | Trna
