Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30 | Zendy

Leijonmarck Marie | Zendy; Appelt Krzysztof | Zendy; Badger John | Zendy; Liljas Anders | Zendy; Wilson Keith S. | Zendy; White Stephen W. | Zendy

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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.

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