2SOB

SN-OB, OB-FOLD SUB-DOMAIN OF STAPHYLOCOCCAL NUCLEASE, NMR, 10 STRUCTURES

「1SOB」から置き換えられました

2SOB の概要

• エントリーDOI: 10.2210/pdb2sob/pdb
• 分子名称: STAPHYLOCOCCAL NUCLEASE (1 entity in total)
• 機能のキーワード: hydrolase (phosphoric diester)
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Nuclease A: Secreted. Nuclease B: Membrane: P00644
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11626.58

構造登録者

Alexandrescu, A.T.,Gittis, A.G.,Abeygunawardana, C.,Shortle, D. (登録日: 1995-09-15, 公開日: 1995-12-07, 最終更新日: 2024-05-22)

主引用文献

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

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: 7608966
DOI: 10.1006/jmbi.1995.0365

実験手法

SOLUTION NMR