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2fvo

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[[Image:2fvo.gif|left|200px]]
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[[Image:2fvo.png|left|200px]]
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{{STRUCTURE_2fvo| PDB=2fvo | SCENE= }}
{{STRUCTURE_2fvo| PDB=2fvo | SCENE= }}
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'''Docking of the modified RF1 X-ray structure into the Low Resolution Cryo-EM map of E.coli 70S Ribosome bound with RF1'''
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===Docking of the modified RF1 X-ray structure into the Low Resolution Cryo-EM map of E.coli 70S Ribosome bound with RF1===
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==Overview==
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In eubacteria, termination of translation is signaled by any one of the stop codons UAA, UAG, and UGA moving into the ribosomal A site. Two release factors, RF1 and RF2, recognize and bind to the stop codons with different affinities and trigger the hydrolysis of the ester bond that links the polypeptide with the P-site tRNA. Cryo-electron microscopy (cryo-EM) results obtained in this study show that ribosome-bound RF1 is in an open conformation, unlike the closed conformation observed in the crystal structure of the free factor, allowing its simultaneous access to both the decoding center and the peptidyl-transferase center. These results are similar to those obtained for RF2, but there is an important difference in how the factors bind to protein L11, which forms part of the GTPase-associated center of the large ribosomal subunit. The difference in the binding position, C-terminal domain for RF2 versus N-terminal domain for RF1, explains a body of L11 mutation studies that revealed differential effects on the activity of the two factors. Very recent data obtained with small-angle X-ray scattering now reveal that the solution structure of RF1 is open, as here seen on the ribosome by cryo-EM, and not closed, as seen in the crystal.
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The line below this paragraph, {{ABSTRACT_PUBMED_16476444}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16476444 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16476444}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM., Rawat U, Gao H, Zavialov A, Gursky R, Ehrenberg M, Frank J, J Mol Biol. 2006 Apr 7;357(4):1144-53. Epub 2006 Jan 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16476444 16476444]
Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM., Rawat U, Gao H, Zavialov A, Gursky R, Ehrenberg M, Frank J, J Mol Biol. 2006 Apr 7;357(4):1144-53. Epub 2006 Jan 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16476444 16476444]
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Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome., Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R, Kim SH, J Mol Biol. 2004 Jul 30;341(1):227-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15312775 15312775]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Zavialov, A.]]
[[Category: Zavialov, A.]]
[[Category: Rf1 ribosome cryo-em]]
[[Category: Rf1 ribosome cryo-em]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:21:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:51:19 2008''

Revision as of 11:51, 29 July 2008

Image:2fvo.png

Template:STRUCTURE 2fvo

Docking of the modified RF1 X-ray structure into the Low Resolution Cryo-EM map of E.coli 70S Ribosome bound with RF1

Template:ABSTRACT PUBMED 16476444

About this Structure

2FVO is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM., Rawat U, Gao H, Zavialov A, Gursky R, Ehrenberg M, Frank J, J Mol Biol. 2006 Apr 7;357(4):1144-53. Epub 2006 Jan 30. PMID:16476444

Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome., Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R, Kim SH, J Mol Biol. 2004 Jul 30;341(1):227-39. PMID:15312775

Page seeded by OCA on Tue Jul 29 14:51:19 2008

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