2bcw

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'''Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex'''<br />
'''Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex'''<br />
==Overview==
==Overview==
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During tRNA translocation on the ribosome, an arc-like connection (ALC) is, formed between the G' domain of elongation factor G (EF-G) and the, L7/L12-stalk base of the large ribosomal subunit in the GDP state. To, delineate the boundary of EF-G within the ALC, we tagged an amino acid, residue near the tip of the G' domain of EF-G with undecagold, which was, then visualized with three-dimensional cryo-electron microscopy (cryo-EM)., Two distinct positions for the undecagold, observed in the GTP-state and, GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine, the movement of the labeled amino acid. Molecular analyses of the cryo-EM, maps show: (1) that three structural components, the N-terminal domain of, ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2), that both EF-G and the ribosomal protein L7/L12 undergo large, conformational changes to form the ALC.
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During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC.
==About this Structure==
==About this Structure==
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2BCW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BCW OCA].
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2BCW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCW OCA].
==Reference==
==Reference==
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Agrawal, R.K.]]
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[[Category: Agrawal, R K.]]
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[[Category: Datta, P.P.]]
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[[Category: Datta, P P.]]
[[Category: Frank, J.]]
[[Category: Frank, J.]]
[[Category: Qi, L.]]
[[Category: Qi, L.]]
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[[Category: Sharma, M.R.]]
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[[Category: Sharma, M R.]]
[[Category: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome]]
[[Category: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:44:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:26 2008''

Revision as of 14:36, 21 February 2008


2bcw

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Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex

Overview

During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC.

About this Structure

2BCW is a Protein complex structure of sequences from Escherichia coli, Thermotoga maritima and Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM., Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK, Mol Cell. 2005 Dec 9;20(5):723-31. PMID:16337596

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