1s1h

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[[Image:1s1h.gif|left|200px]]
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{{STRUCTURE_1s1h| PDB=1s1h | SCENE= }}
{{STRUCTURE_1s1h| PDB=1s1h | SCENE= }}
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'''Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map. This file, 1S1H, Contains 40S subunit. The 60S Ribosomal Subunit Is In File 1S1I.'''
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===Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map. This file, 1S1H, Contains 40S subunit. The 60S Ribosomal Subunit Is In File 1S1I.===
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==Overview==
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An 11.7-A-resolution cryo-EM map of the yeast 80S.eEF2 complex in the presence of the antibiotic sordarin was interpreted in molecular terms, revealing large conformational changes within eEF2 and the 80S ribosome, including a rearrangement of the functionally important ribosomal intersubunit bridges. Sordarin positions domain III of eEF2 so that it can interact with the sarcin-ricin loop of 25S rRNA and protein rpS23 (S12p). This particular conformation explains the inhibitory action of sordarin and suggests that eEF2 is stalled on the 80S ribosome in a conformation that has similarities with the GTPase activation state. A ratchet-like subunit rearrangement (RSR) occurs in the 80S.eEF2.sordarin complex that, in contrast to Escherichia coli 70S ribosomes, is also present in vacant 80S ribosomes. A model is suggested, according to which the RSR is part of a mechanism for moving the tRNAs during the translocation reaction.
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(as it appears on PubMed at http://www.pubmed.gov), where 14976550 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14976550}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation., Spahn CM, Gomez-Lorenzo MG, Grassucci RA, Jorgensen R, Andersen GR, Beckmann R, Penczek PA, Ballesta JP, Frank J, EMBO J. 2004 Mar 10;23(5):1008-19. Epub 2004 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14976550 14976550]
Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation., Spahn CM, Gomez-Lorenzo MG, Grassucci RA, Jorgensen R, Andersen GR, Beckmann R, Penczek PA, Ballesta JP, Frank J, EMBO J. 2004 Mar 10;23(5):1008-19. Epub 2004 Feb 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14976550 14976550]
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EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome., Agrawal RK, Heagle AB, Penczek P, Grassucci RA, Frank J, Nat Struct Biol. 1999 Jul;6(7):643-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10404220 10404220]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Sordarin]]
[[Category: Sordarin]]
[[Category: Trna translocation]]
[[Category: Trna translocation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:10:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:08:14 2008''

Revision as of 15:08, 27 July 2008

Template:STRUCTURE 1s1h

Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map. This file, 1S1H, Contains 40S subunit. The 60S Ribosomal Subunit Is In File 1S1I.

Template:ABSTRACT PUBMED 14976550

About this Structure

1S1H is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation., Spahn CM, Gomez-Lorenzo MG, Grassucci RA, Jorgensen R, Andersen GR, Beckmann R, Penczek PA, Ballesta JP, Frank J, EMBO J. 2004 Mar 10;23(5):1008-19. Epub 2004 Feb 19. PMID:14976550

EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome., Agrawal RK, Heagle AB, Penczek P, Grassucci RA, Frank J, Nat Struct Biol. 1999 Jul;6(7):643-7. PMID:10404220

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