Structural highlights
Function
[RL7_ECOLI] Seems to be the binding site for several of the factors involved in protein synthesis and appears to be essential for accurate translation.[HAMAP-Rule:MF_00368]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.
Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A.,Leijonmarck M, Liljas A J Mol Biol. 1987 Jun 5;195(3):555-79. PMID:3309338[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leijonmarck M, Liljas A. Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A. J Mol Biol. 1987 Jun 5;195(3):555-79. PMID:3309338
