Publication Abstract from PubMed
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.
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.,Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG Cell. 1997 Jan 24;88(2):235-42. PMID:9008164[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
