5XEU

crystal structure of Hcp2 from Salmonella typhimurium

Summary for 5XEU

• Entry DOI: 10.2210/pdb5xeu/pdb
• Descriptor: Hcp1 family type VI secretion system effector (1 entity in total)
• Functional Keywords: hexameric, cytosolic protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 6
• Total formula weight: 106499.31

Authors

Lin, Q.P.,Gao, Z.Q.,Zhang, H. (deposition date: 2017-04-06, release date: 2017-08-16, Last modification date: 2023-11-22)

Primary citation

Lin, Q.P.,Gao, Z.Q.,Geng, Z.,Zhang, H.,Dong, Y.H.
Crystal structure of the putative cytoplasmic protein STM0279 (Hcp2) from Salmonella typhimurium
Acta Crystallogr F Struct Biol Commun, 73:463-468, 2017

PubMed Abstract: STM0279 is a putative cytoplasmic protein from Salmonella typhimurium and was recently renamed haemolysin co-regulated protein 2 (Hcp2), with the neighbouring STM0276 being Hcp1. Both of them are encoded by the type VI secretion system (T6SS) of the Salmonella pathogenicity island 6 (SPI-6) locus and have high sequence identity. The Hcp proteins may function as a vital component of the T6SS nanotube and as a transporter and chaperone of diverse effectors from the bacterial T6SS. 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.

PubMed: 28777089
DOI: 10.1107/S2053230X17010512

Experimental method

X-RAY DIFFRACTION (3 Å)