2sob
From Proteopedia
SN-OB, OB-FOLD SUB-DOMAIN OF STAPHYLOCOCCAL NUCLEASE, NMR, 10 STRUCTURES
Overview
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.
About this Structure
2SOB is a Single protein structure of sequence from Staphylococcus aureus. This structure supersedes the now removed PDB entry 1sob. Full crystallographic information is available from OCA.
Reference
NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease., Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D, J Mol Biol. 1995 Jul 7;250(2):134-43. PMID:7608966 Page seeded by OCA on Sun May 4 17:20:20 2008
