2XGR

extracellular endonuclease

Summary for 2XGR

• Entry DOI: 10.2210/pdb2xgr/pdb
• Descriptor: SPD1 NUCLEASE, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: hydrolase, metal binding
• Biological source: STREPTOCOCCUS PYOGENES SEROTYPE M1
• Total number of polymer chains: 1
• Total formula weight: 29249.72

Authors

Korczynska, J.E.,Turkenburg, J.P.,Taylor, E.J. (deposition date: 2010-06-07, release date: 2011-07-20, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)