Summary for 2SOB
| Entry DOI | 10.2210/pdb2sob/pdb |
| Descriptor | STAPHYLOCOCCAL NUCLEASE (1 entity in total) |
| Functional Keywords | hydrolase (phosphoric diester) |
| Biological source | Staphylococcus aureus |
| Cellular location | Nuclease A: Secreted. Nuclease B: Membrane: P00644 |
| Total number of polymer chains | 1 |
| Total formula weight | 11626.58 |
| Authors | Alexandrescu, A.T.,Gittis, A.G.,Abeygunawardana, C.,Shortle, D. (deposition date: 1995-09-15, release date: 1995-12-07, Last modification date: 2024-05-22) |
| Primary citation | Alexandrescu, A.T.,Gittis, A.G.,Abeygunawardana, C.,Shortle, D. NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease. J.Mol.Biol., 250:134-143, 1995 Cited by PubMed Abstract: Similar folds often occur in proteins with dissimilar sequences. The OB-fold forms a part of the structures of at least seven non-homologous proteins that share either oligonucleotide or oligosaccharide binding functions. A 1-103 fragment corresponding to the OB-fold of the 149 amino acid residue staphylococcal nuclease gives NMR spectra characteristic of an unfolded protein, i.e. the wild-type nuclease sequence is insufficient to maintain a stable tertiary structure in the absence of the C-terminal one-third of this single-domain protein. By contrast, the 1-103 fragment of nuclease with the mutations Val66Leu and Gly88Val adopts a stable tertiary structure. The NMR solution structure of this latter fragment is a close variation of the OB-fold found in the X-ray structure of the parent protein. The Val66Leu and Gly88Val mutations appear to stabilize tertiary structure by consolidating the hydrophobic core of the nuclease OB-fold sub-domain. Taken together, these results suggest that recurrent structural motifs such as the OB-fold may in some cases represent vestiges of autonomous folding units that, during evolution, have become integrated into more complex cooperative folding domains. PubMed: 7608966DOI: 10.1006/jmbi.1995.0365 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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