1ond

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(New page: 200px<br /><applet load="1ond" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ond, resolution 3.40&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1ond.gif|left|200px]]<br /><applet load="1ond" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ond, resolution 3.40&Aring;" />
caption="1ond, resolution 3.40&Aring;" />
'''THE CRYSTAL STRUCTURE OF THE 50S LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS COMPLEXED WITH TROLEANDOMYCIN MACROLIDE ANTIBIOTIC'''<br />
'''THE CRYSTAL STRUCTURE OF THE 50S LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS COMPLEXED WITH TROLEANDOMYCIN MACROLIDE ANTIBIOTIC'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1OND is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with TAO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OND OCA].
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1OND is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=TAO:'>TAO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OND OCA].
==Reference==
==Reference==
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[[Category: trna]]
[[Category: trna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:02:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:35 2008''

Revision as of 12:19, 21 February 2008

Image:1ond.gif

1ond, resolution 3.40Å

Drag the structure with the mouse to rotate

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 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

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