Crystal structure of the putative cytoplasmic protein STM0279 (Hcp2) from Salmonella typhimurium

In this study, the crystal structure and the oligomeric state in solution of Hcp2 from S. typhimurium (StHcp2) were investigated. The crystal structure refined to 3.0   Å resolution showed that the protein is composed of a β -barrel domain with extended loops and can form hexameric rings as observed in known Hcp homologues. Mutation of the extended loop was found to partly destabilize the hexameric conformation into monomers or cause the production of inclusion bodies, suggesting it has an important role in hexameric ring formation.

Source: Acta Crystallographica Section F - July 26, 2017 Category: Biochemistry Authors: Lin, Q.-P. Gao, Z.-Q. Geng, Z. Zhang, H. Dong, Y.-H. Tags: type VI secretion system crystal structure haemolysin co-regulated protein hexameric rings T6SS assembly research communications Source Type: research