3K55

Structure of beta hairpin deletion mutant of beta toxin from Staphylococcus aureus

3K55 の概要

• エントリーDOI: 10.2210/pdb3k55/pdb
• 分子名称: Beta-hemolysin, CHLORIDE ION, SODIUM ION (3 entities in total)
• 機能のキーワード: beta toxin, hemolysin, sphingomyelinase, domain swapping, hydrolase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 556124.79

構造登録者

Kruse, A.C.,Huseby, M.,Shi, K.,Digre, J.,Ohlendorf, D.H.,Earhart, C.A. (登録日: 2009-10-06, 公開日: 2011-01-26, 最終更新日: 2024-11-20)

主引用文献

Kruse, A.C.,Huseby, M.J.,Shi, K.,Digre, J.,Ohlendorf, D.H.,Earhart, C.A.
Structure of a mutant beta toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility
Acta Crystallogr.,Sect.F, 67:438-441, 2011

PubMed Abstract: The 3.35 Å resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase β toxin in which a conserved hydrophobic β-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal β-strand, leading to the formation of dimers linked by a conformationally flexible hinge region. Eight dimers are seen in the asymmetric unit, exhibiting a broad spectrum of conformations trapped in place by intermolecular contacts within the crystal lattice. Furthermore, the 16 monomers within each asymmetric unit exhibit a remarkable heterogeneity in thermal factors, which can be accounted for by the varying degrees to which each monomer interacts with other molecules in the crystal. This structure provides a unique example of the challenges associated with crystallographic study of flexible proteins.

PubMed: 21505235
DOI: 10.1107/S1744309111005239

実験手法

X-RAY DIFFRACTION (3.35 Å)