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A model for the spatial arrangement of the proteins in the large subunit of the Escherichia coli ribosome.
Author(s) -
Walleczek J.,
Schüler D.,
StöfflerMeilicke M.,
Brimacombe R.,
Stöffler G.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03234.x
Subject(s) - biology , escherichia coli , ribosome , escherichia coli proteins , protein subunit , bacterial protein , genetics , translation (biology) , computational biology , bacteria , rna , gene , messenger rna
A three‐dimensional model for the arrangement of 29 of the 33 proteins from the Escherichia coli large ribosomal subunit has been generated by interactive computer graphics. The topographical information that served as input in the model building process was obtained by combining the immunoelectron microscopically determined network of epitope‐epitope distances on the surface of the large ribosomal subunit with in situ protein‐protein cross‐linking data. These two independent sets of data were shown to be compatible by geometric analysis, thus allowing the construction of an inherently consistent model. The model shows (i) that the lower third of the large subunit is protein‐poor, (ii) that proteins known to be functionally involved in peptide bond formation and translocation are clustered in two separate regions, (iii) that proteins functionally interdependent during the self‐assembly of the large subunit are close neighbours in the mature subunit and (iv) that proteins forming the early assembly nucleus are grouped together in a distinct region at the ‘back’ of the subunit.