1SRO
S1 RNA BINDING DOMAIN, NMR, 20 STRUCTURES
Summary for 1SRO
| Entry DOI | 10.2210/pdb1sro/pdb |
| Descriptor | PNPASE (1 entity in total) |
| Functional Keywords | s1 rna-binding domain, polynucleotide phosphorylase (pnpase) |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P05055 |
| Total number of polymer chains | 1 |
| Total formula weight | 8380.70 |
| Authors | Bycroft, M. (deposition date: 1996-11-27, release date: 1997-04-01, Last modification date: 2024-05-22) |
| Primary citation | Bycroft, M.,Hubbard, T.J.,Proctor, M.,Freund, S.M.,Murzin, A.G. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell(Cambridge,Mass.), 88:235-242, 1997 Cited by PubMed 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. PubMed: 9008164DOI: 10.1016/S0092-8674(00)81844-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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