2XGR

extracellular endonuclease

2XGR の概要

• エントリーDOI: 10.2210/pdb2xgr/pdb
• 分子名称: SPD1 NUCLEASE, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: hydrolase, metal binding
• 由来する生物種: STREPTOCOCCUS PYOGENES SEROTYPE M1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29249.72

構造登録者

Korczynska, J.E.,Turkenburg, J.P.,Taylor, E.J. (登録日: 2010-06-07, 公開日: 2011-07-20, 最終更新日: 2024-05-08)

主引用文献

Korczynska, J.E.,Turkenburg, J.P.,Taylor, E.J.
The Structural Characterization of a Prophage-Encoded Extracellular DNase from Streptococcus Pyogenes.
Nucleic Acids Res., 40:928-, 2012

PubMed Abstract: The pathogenic bacterium Group A Streptococcus pyogenes produces several extracellular DNases that have been shown to facilitate invasive infection by evading the human host immune system. DNases degrade the chromatin in neutrophil extracellular traps, enabling the bacterium to evade neutrophil capture. Spd1 is a type I, nonspecific ββα/metal-dependent nuclease from Streptococcus pyogenes, which is encoded by the SF370.1 prophage and is likely to be expressed as a result of prophage induction. We present here the X-ray structure of this DNase in the wild-type and Asn145Ala mutant form. Through structural and sequence alignments as well as mutagenesis studies, we have identified the key residues His121, Asn145 and Glu164, which are crucial for Spd1 nucleolytic activity and shown the active site constellation. Our wild-type structure alludes to the possibility of a catalytically blocked dimeric form of the protein. We have investigated the multimeric nature of Spd1 using size-exclusion chromatography with multi-angle light scattering (SEC-MALLS) in the presence and absence of the divalent metal ion Mg(2+), which suggests that Spd1 exists in a monomeric form in solution.

PubMed: 21948797
DOI: 10.1093/NAR/GKR789

実験手法

X-RAY DIFFRACTION (1.7 Å)