Computed spatial homology between the L12 protein of chloroplast ribosome and 1.7 A structure of Escherichia coli L12 domain.
A computer-graphic model of the tertiary structure of a functional domain in an organelle ribosomal protein was generated using the amino acid sequence of chloroplast ribosomal protein L12 from spinach (Bartsch, Kimura and Subramanian, Proc. Natl. Acad. Sci. USA 79, 6871-6875, 1982) and 1.7 A resolution coordinates of the E. coli L12 C-terminal fragment crystal (Leijonmarck, Eriksson and Liljas, Nature 286, 824-826, 1980). A comparison between the model and the experimentally derived structure shows that although 40% of the primary structure of this part of the two proteins has undergone amino acid replacements, the gross spatial structure of the domain is maintained and the character of the surfaces of possible functional importance are not significantly altered.
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000032:analysis*; D003201:Computers; D004926:Escherichia coli / Q000032:analysis*; D008958:Models, Molecular; D010944:Plants / Q000032:analysis; D011487:Protein Conformation; D012269:Ribosomal Proteins; D012270:Ribosomes / Q000032:analysis*; D013045:Species Specificity
D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12