Ribosomal protein L7/L12
From Proteopedia
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{{STRUCTURE_1dd3| PDB=1dd3 | SIZE=400| SCENE=Ribosomal_protein_L7/Cv/1 |right|CAPTION=Ribosomal protein L7/L12 from ''Thermotoga maritima'' [[1dd3]] }} | {{STRUCTURE_1dd3| PDB=1dd3 | SIZE=400| SCENE=Ribosomal_protein_L7/Cv/1 |right|CAPTION=Ribosomal protein L7/L12 from ''Thermotoga maritima'' [[1dd3]] }} | ||
- | [[Ribosomal protein L7]] (RPL7) is one of the 34 proteins which belong to the large 50S subunit of the prokaryotic ribosome or to the ca. 49 proteins in the large 60S subunit of the eukaryotic ribosome. It is part of the L7/L12 complex. Two dimers of L7/L12 are present in the large subunit. The L7/L12 probably interacts with EF-Tu. L7 and L12 differ by one post-translational modification at the N-terminal of L7. In the archaea, the L7Ae acts as a subunit of RNase P. | + | [[Ribosomal protein L7]] (RPL7) is one of the 34 proteins which belong to the large 50S subunit of the prokaryotic ribosome or to the ca. 49 proteins in the large 60S subunit of the eukaryotic ribosome. It is part of the L7/L12 complex. Two dimers of L7/L12 are present in the large subunit. The L7/L12 probably interacts with EF-Tu. L7 and L12 differ by one post-translational modification at the N-terminal of L7. In the archaea, the L7Ae acts as a subunit of RNase P. For more details see [[15.5kD/Snu13/L7Ae]]. |
== 3D Structures of Ribosomal protein L7 == | == 3D Structures of Ribosomal protein L7 == |
Revision as of 09:11, 27 January 2016
Ribosomal protein L7 (RPL7) is one of the 34 proteins which belong to the large 50S subunit of the prokaryotic ribosome or to the ca. 49 proteins in the large 60S subunit of the eukaryotic ribosome. It is part of the L7/L12 complex. Two dimers of L7/L12 are present in the large subunit. The L7/L12 probably interacts with EF-Tu. L7 and L12 differ by one post-translational modification at the N-terminal of L7. In the archaea, the L7Ae acts as a subunit of RNase P. For more details see 15.5kD/Snu13/L7Ae.
3D Structures of Ribosomal protein L7
Updated on 27-January-2016
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