1jqs

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(New page: 200px<br /><applet load="1jqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqs" /> '''Fitting of L11 protein and elongation factor...)
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'''Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog'''<br />
'''Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog'''<br />
==Overview==
==Overview==
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L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit, of the Escherichia coli ribosome. Because of the flexible nature of the, region, recent X-ray crystallographic studies of the 50 S subunit failed, to locate the N-terminal domain of the protein. We have determined the, position of the complete L11 protein by comparing a three-dimensional, cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant, lacking ribosomal protein L11, with the three-dimensional map of the, wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA, complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G, intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal, domain of L11 (where the antibiotic thiostrepton binds), causing the, N-terminal domain to move and thereby inducing the formation of the, arc-like connection with the G' domain of EF-G. The results provide a new, insight into the mechanism of EF-G-dependent translocation.
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L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit of the Escherichia coli ribosome. Because of the flexible nature of the region, recent X-ray crystallographic studies of the 50 S subunit failed to locate the N-terminal domain of the protein. We have determined the position of the complete L11 protein by comparing a three-dimensional cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant lacking ribosomal protein L11, with the three-dimensional map of the wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal domain of L11 (where the antibiotic thiostrepton binds), causing the N-terminal domain to move and thereby inducing the formation of the arc-like connection with the G' domain of EF-G. The results provide a new insight into the mechanism of EF-G-dependent translocation.
==About this Structure==
==About this Structure==
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1JQS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQS OCA].
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1JQS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQS OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Agrawal, R.K.]]
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[[Category: Agrawal, R K.]]
[[Category: Frank, J.]]
[[Category: Frank, J.]]
[[Category: Linde, J.]]
[[Category: Linde, J.]]
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[[Category: Nierhaus, K.H.]]
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[[Category: Nierhaus, K H.]]
[[Category: Segupta, J.]]
[[Category: Segupta, J.]]
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[[Category: 70s e.coli ribosome]]
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[[Category: 70s e coli ribosome]]
[[Category: cryo-em]]
[[Category: cryo-em]]
[[Category: ef-g]]
[[Category: ef-g]]
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[[Category: l11]]
[[Category: l11]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:29:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:46 2008''

Revision as of 11:25, 21 February 2008


1jqs

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Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog

Overview

L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit of the Escherichia coli ribosome. Because of the flexible nature of the region, recent X-ray crystallographic studies of the 50 S subunit failed to locate the N-terminal domain of the protein. We have determined the position of the complete L11 protein by comparing a three-dimensional cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant lacking ribosomal protein L11, with the three-dimensional map of the wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal domain of L11 (where the antibiotic thiostrepton binds), causing the N-terminal domain to move and thereby inducing the formation of the arc-like connection with the G' domain of EF-G. The results provide a new insight into the mechanism of EF-G-dependent translocation.

About this Structure

1JQS is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation., Agrawal RK, Linde J, Sengupta J, Nierhaus KH, Frank J, J Mol Biol. 2001 Aug 24;311(4):777-87. PMID:11518530

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