S1 ___domain

The S1 ___domain is a protein ___domain that was originally identified in ribosomal protein S1 but is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding ___domain from the Escherichia 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.^[2]

S1 ___domain
Crystal structure of the S1 ___domain of RNase E from E. coli (Pb derivative).[1]
Identifiers
Symbol	S1
Pfam	PF00575
Pfam clan	CL0021
InterPro	IPR003029
SMART	S1
PROSITE	PDOC00053
MEROPS	S15
SCOP2	1sro / SCOPe / SUPFAM
CDD	cd00164
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1sn8​

The structure of the S1 ___domain is very similar to that of cold shock proteins. This suggests that they may both be derived from an ancient nucleic acid-binding protein.^[2]

Function

The S1 ___domain is an essential in protein translation as it interacts with the ribosome and messenger RNA. S1 bind to RNA in a sequence specific manner.

Structure

This protein ___domain contains six motifs and 70 amino acids and it folds into a five-stranded antiparallel beta barrel. The structure of the S1 ___domain is very similar to that of cold shock proteins. This suggests that they may both be derived from an ancient nucleic acid-binding protein. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site.^[2]

References

1. Schubert M, Edge RE, Lario P, et al. (July 2004). "Structural characterization of the RNase E S1 ___domain and identification of its oligonucleotide-binding and dimerization interfaces". J. Mol. Biol. 341 (1): 37–54. CiteSeerX 10.1.1.513.8431. doi:10.1016/j.jmb.2004.05.061. PMID 15312761.
2. Bycroft M, Hubbard TJ, Proctor M, Freund SM, Murzin AG (January 1997). "The solution structure of the S1 RNA binding ___domain: a member of an ancient nucleic acid-binding fold". Cell. 88 (2): 235–42. doi:10.1016/S0092-8674(00)81844-9. PMID 9008164. S2CID 9623142.

This article incorporates text from the public ___domain Pfam and InterPro: IPR003029