1pn6
From Proteopedia
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| - | [[Image:1pn6.gif|left|200px]]<br /><applet load="1pn6" size=" | + | [[Image:1pn6.gif|left|200px]]<br /><applet load="1pn6" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.'''<br /> | '''Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | During the ribosomal translocation, the binding of elongation factor G | + | During the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the 50S subunit in the direction of the mRNA movement. By means of cryo-electron microscopy we observe that this rotation is accompanied by a 20 A movement of the L1 stalk of the 50S subunit, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site. These ribosomal motions can occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer to the A-site tRNA or peptide removal, the presence of the charged P-site tRNA locks the ribosome and prohibits both of these motions. |
==About this Structure== | ==About this Structure== | ||
| - | 1PN6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1PN6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Zavialov, A.]] | [[Category: Zavialov, A.]] | ||
[[Category: cryo-em]] | [[Category: cryo-em]] | ||
| - | [[Category: e | + | [[Category: e coli 70s ribosome]] |
[[Category: elongation factor-g]] | [[Category: elongation factor-g]] | ||
[[Category: fitting of crystal structure]] | [[Category: fitting of crystal structure]] | ||
[[Category: post-termination complex]] | [[Category: post-termination complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:28 2008'' |
Revision as of 12:30, 21 February 2008
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Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.
Overview
During the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation of the 30S subunit relative to the 50S subunit in the direction of the mRNA movement. By means of cryo-electron microscopy we observe that this rotation is accompanied by a 20 A movement of the L1 stalk of the 50S subunit, implying that this region is involved in the translocation of deacylated tRNAs from the P to the E site. These ribosomal motions can occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer to the A-site tRNA or peptide removal, the presence of the charged P-site tRNA locks the ribosome and prohibits both of these motions.
About this Structure
1PN6 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Locking and unlocking of ribosomal motions., Valle M, Zavialov A, Sengupta J, Rawat U, Ehrenberg M, Frank J, Cell. 2003 Jul 11;114(1):123-34. PMID:12859903
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