1ml5: Difference between revisions

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New page: left|200px<br /><applet load="1ml5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ml5" /> '''Structure of the E. coli ribosomal terminati...
 
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[[Image:1ml5.gif|left|200px]]<br /><applet load="1ml5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ml5.gif|left|200px]]<br /><applet load="1ml5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ml5" />
caption="1ml5" />
'''Structure of the E. coli ribosomal termination complex with release factor 2'''<br />
'''Structure of the E. coli ribosomal termination complex with release factor 2'''<br />


==Overview==
==Overview==
Termination of protein synthesis occurs when the messenger RNA presents a, stop codon in the ribosomal aminoacyl (A) site. Class I release factor, proteins (RF1 or RF2) are believed to recognize stop codons via tripeptide, motifs, leading to release of the completed polypeptide chain from its, covalent attachment to transfer RNA in the ribosomal peptidyl (P) site., Class I RFs possess a conserved GGQ amino-acid motif that is thought to be, involved directly in protein-transfer-RNA bond hydrolysis. Crystal, structures of bacterial and eukaryotic class I RFs have been determined, but the mechanism of stop codon recognition and peptidyl-tRNA hydrolysis, remains unclear. Here we present the structure of the Escherichia coli, ribosome in a post-termination complex with RF2, obtained by, single-particle cryo-electron microscopy (cryo-EM). Fitting the known 70S, and RF2 structures into the electron density map reveals that RF2 adopts a, different conformation on the ribosome when compared with the crystal, structure of the isolated protein. The amino-terminal helical domain of, RF2 contacts the factor-binding site of the ribosome, the 'SPF' loop of, the protein is situated close to the mRNA, and the GGQ-containing domain, of RF2 interacts with the peptidyl-transferase centre (PTC). By connecting, the ribosomal decoding centre with the PTC, RF2 functionally mimics a tRNA, molecule in the A site. Translational termination in eukaryotes is likely, to be based on a similar mechanism.
Termination of protein synthesis occurs when the messenger RNA presents a stop codon in the ribosomal aminoacyl (A) site. Class I release factor proteins (RF1 or RF2) are believed to recognize stop codons via tripeptide motifs, leading to release of the completed polypeptide chain from its covalent attachment to transfer RNA in the ribosomal peptidyl (P) site. Class I RFs possess a conserved GGQ amino-acid motif that is thought to be involved directly in protein-transfer-RNA bond hydrolysis. Crystal structures of bacterial and eukaryotic class I RFs have been determined, but the mechanism of stop codon recognition and peptidyl-tRNA hydrolysis remains unclear. Here we present the structure of the Escherichia coli ribosome in a post-termination complex with RF2, obtained by single-particle cryo-electron microscopy (cryo-EM). Fitting the known 70S and RF2 structures into the electron density map reveals that RF2 adopts a different conformation on the ribosome when compared with the crystal structure of the isolated protein. The amino-terminal helical domain of RF2 contacts the factor-binding site of the ribosome, the 'SPF' loop of the protein is situated close to the mRNA, and the GGQ-containing domain of RF2 interacts with the peptidyl-transferase centre (PTC). By connecting the ribosomal decoding centre with the PTC, RF2 functionally mimics a tRNA molecule in the A site. Translational termination in eukaryotes is likely to be based on a similar mechanism.


==About this Structure==
==About this Structure==
1ML5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1ML5 OCA].  
1ML5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1ML5 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ehrenberg, M.]]
[[Category: Ehrenberg, M.]]
[[Category: Heel, M.van.]]
[[Category: Heel, M van.]]
[[Category: Klaholz, B.P.]]
[[Category: Klaholz, B P.]]
[[Category: Myasnikov, A.G.]]
[[Category: Myasnikov, A G.]]
[[Category: Orlova, E.V.]]
[[Category: Orlova, E V.]]
[[Category: Pape, T.]]
[[Category: Pape, T.]]
[[Category: Vestergaard, B.]]
[[Category: Vestergaard, B.]]
[[Category: Zavialov, A.V.]]
[[Category: Zavialov, A V.]]
[[Category: angular reconstitution]]
[[Category: angular reconstitution]]
[[Category: cryo-eletron microscopy]]
[[Category: cryo-eletron microscopy]]
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[[Category: termination of protein synthesis]]
[[Category: termination of protein synthesis]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:29:43 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:18 2008''