|PROSITE documentation PDOC50126|
The S1 domain of around 70 amino acids, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. It has been shown that S1 proteins bind RNA through their S1 domains with some degree of sequence specificity [1,2].
The solution structure of one S1 RNA-binding domain from Escherichia coli polynucleotide phosphorylase has been determined . It displays some similarity with the cold shock domain (CSD) (see <PDOC00304>). Both the S1 and the CSD domain consist of an antiparallel β barrel of the same topology with 5 β strands. This fold is also shared by many other proteins of unrelated function and is known as the OB fold . However, the S1 and CSD fold can be distinguished from the other OB folds by the presence of a short 3(10) helix at the end of strand 3. This unique feature is likely to form a part of the DNA/RNA-binding site .
Some of the proteins in which an S1 domain is found are listed below.
To identify S1 domains we developed 2 profiles, one is specific for bacterial, chloroplastic and eukaryotic IF-1 proteins. The other recognize all other S1 domains. Both profiles cover the whole domain.Last update:
December 2001 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Boni I.V., Isaeva D.M., Musychenko M.L., Tzareva N.V.|
|Title||Ribosome-messenger recognition: mRNA target sites for ribosomal protein S1.|
|Source||Nucleic Acids Res. 19:155-162(1991).|
|2||Authors||Ringquist S., Jones T., Snyder E.E., Gibson T., Boni I., Gold L.|
|Title||High-affinity RNA ligands to Escherichia coli ribosomes and ribosomal protein S1: comparison of natural and unnatural binding sites.|
|3||Authors||Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G.|
|Title||The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.|
|Title||OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.|
|Source||EMBO J. 12:861-867(1993).|