The Solution Structure of the S1 RNA Binding Domain: A Member of an Ancient Nucleic Acid–Binding Fold
CellPublished 1 January 1997Open access
Mark Bycroft, Tim Hubbard, Mark R. Proctor, Stefan M.V. Freund, Alexey G. Murzin
Citations412
SJR quartileQ1
SJR score22.61
SNIP7.62
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TL;DR
Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins, suggesting that they are both derived from an ancient nucleic acid-binding protein.
Abstract
The S1 domain, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the E. coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site. The structure of the S1 domain is very similar to that of cold shock protein, suggesting that they are both derived from an ancient nucleic acid-binding protein. Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins.
Keywords
Biochemistry, Genetics and Molecular Biology
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