The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.
作者： Mark Bycroft , Tim J.P Hubbard , Mark Proctor , Stefan M.V Freund , Alexey G Murzin
DOI: 10.1016/S0092-8674(00)81844-9
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摘要: Abstract The S1 domain, originally identified in ribosomal protein S1, is found a large number of RNA-associated proteins. structure the RNA-binding domain from E. coli polynucleotide phosphorylase has been determined using NMR methods and consists five-stranded antiparallel β barrel. Conserved residues on one face barrel adjacent loops form putative site. very similar to that cold shock protein, suggesting they are both derived an ancient nucleic acid–binding protein. Enhanced sequence searches reveal hitherto unidentified domains RNase E, II, NusA, EMB-5, other
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