Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins.

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 Res

journal_title

Nucleic acids research

authors

Rice PA,Steitz TA

doi

10.1093/nar/17.10.3757

subject

Has Abstract

pub_date

1989-05-25 00:00:00

pages

3757-62

issue

10

eissn

0305-1048

issn

1362-4962

journal_volume

17

pub_type

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