4XZ7

Crystal structure of a TGase

Summary for 4XZ7

• Entry DOI: 10.2210/pdb4xz7/pdb
• Descriptor: Putative uncharacterized protein (2 entities in total)
• Functional Keywords: tgase acitivy, homodimer, anti-phacocytosis, virulence factor, transferase
• Biological source: Streptococcus suis
• Total number of polymer chains: 2
• Total formula weight: 91474.04

Authors

Yu, J.,Ge, J.,Yang, M. (deposition date: 2015-02-04, release date: 2015-06-24, Last modification date: 2024-03-20)

Primary citation

Yu, J.,Pian, Y.,Ge, J.,Guo, J.,Zheng, Y.,Jiang, H.,Hao, H.,Yuan, Y.,Jiang, Y.,Yang, M.
Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis
J.Biol.Chem., 290:19081-19092, 2015

PubMed Abstract: Streptococcus suis serotype 2 (Ss2) is an important swine and human zoonotic pathogen. In the present study, we identified a novel secreted immunogenic protein, SsTGase, containing a highly conserved eukaryotic-like transglutaminase (TGase) domain at the N terminus. We found that inactivation of SsTGase significantly reduced the virulence of Ss2 in a pig infection model and impaired its antiphagocytosis in human blood. We further solved the crystal structure of the N-terminal portion of the protein in homodimer form at 2.1 Å. Structure-based mutagenesis and biochemical studies suggested that disruption of the homodimer directly resulted in the loss of its TGase activity and antiphagocytic ability. Characterization of SsTGase as a novel virulence factor of Ss2 by acting as a TGase would be beneficial for developing new therapeutic agents against Ss2 infections.

PubMed: 26085092
DOI: 10.1074/jbc.M115.643338

Experimental method

X-RAY DIFFRACTION (2.101 Å)