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Cell. 1997 Jan 24;88(2):235-42.

The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.

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1
Department of Chemistry, University of Cambridge, United Kingdom.

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.

PMID:
9008164
DOI:
10.1016/s0092-8674(00)81844-9
[Indexed for MEDLINE]
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