Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A.
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.
Leijonmarck
M
M
Institute of Molecular Biology, University of Uppsala, Sweden.
Liljas
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003461:Crystallography; D004926:Escherichia coli / Q000032:analysis; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D012269:Ribosomal Proteins
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12