Abstract:
:Inspection of the structure of the C-terminal domain of ribosomal protein L7/L12 (1) reveals a helix-turn-helix motif similar to the one found in many DNA-binding regulatory proteins (2-5). The 19 alpha-carbon atoms of the L7/L12 alpha-helices superimpose on the DNA binding helices of CAP and cro with root-mean-square distances between corresponding alpha carbons of 1.45 and 1.55 A, respectively. These helices in L7/L12 are within a patch of highly conserved residues on the surface of L7/L12 whose role is as yet uncertain. We raise the possibility that they may constitute a binding site for nucleic acids, most probably RNA. Consistent with this hypothesis are calculations of the electrostatic charge potential surrounding the protein, which show a region of positive potential centered on the first of these helices.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Rice PA,Steitz TAdoi
10.1093/nar/17.10.3757subject
Has Abstractpub_date
1989-05-25 00:00:00pages
3757-62issue
10eissn
0305-1048issn
1362-4962journal_volume
17pub_type
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