1pn7: Difference between revisions

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New page: left|200px<br /><applet load="1pn7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn7" /> '''Coordinates of S12, L11 proteins and P-tRNA,...
 
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[[Image:1pn7.gif|left|200px]]<br /><applet load="1pn7" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1pn7.gif|left|200px]]<br /><applet load="1pn7" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1pn7" />
caption="1pn7" />
'''Coordinates of S12, L11 proteins and P-tRNA, from the 70S X-ray structure aligned to the 70S Cryo-EM map of E.coli ribosome'''<br />
'''Coordinates of S12, L11 proteins and P-tRNA, from the 70S X-ray structure aligned to the 70S Cryo-EM map of E.coli ribosome'''<br />


==Overview==
==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.
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==
1PN7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [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=1PN7 OCA].  
1PN7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [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=1PN7 OCA].  


==Reference==
==Reference==
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[[Category: trna binding protein]]
[[Category: trna binding protein]]


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