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Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30
Author(s) -
Leijonmarck Marie,
Appelt Krzysztof,
Badger John,
Liljas Anders,
Wilson Keith S.,
White Stephen W.
Publication year - 1988
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340030405
Subject(s) - antiparallel (mathematics) , ribosomal protein , crystallography , ribosomal rna , similarity (geometry) , chemistry , biology , ribosome , physics , biochemistry , computer science , rna , quantum mechanics , magnetic field , gene , artificial intelligence , image (mathematics)
The structure of two prokaryotic ribosomal proteins, the carboxyterminal half of L7/L12 from Escherichia coli (L12CTF) and 1.30 from Bacilus Stearothermophilus display a remarkably similar fold in which alpaha‐helices pack onto one side of an antiparallel, three‐stranded, beta‐pleated sheet. A detailed comparison of the structures by least‐squares methods reveals that more than two‐thirds of the alpha carbons can be superimposed with a root mean square distance of 2.33 Å. The principal difference is an extra alpha‐helix in L12 CTF. The sequences of the proteins display a distinct conservation in regions which are crucial to the common fold, in particular the hydrophobic core. It is proposed that the similarity is a result of divergent evolution.