5IO8

Salmonella Typhimurium VirG-like (STV) protein at 2.19 Angstrom resolution solved by Iodine SAD.

Summary for 5IO8

• Entry DOI: 10.2210/pdb5io8/pdb
• Descriptor: VirG-like protein, IODIDE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: ltxxq motif, cpxp_like family, virg-like protein, unknown function
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (Salmonella typhimurium SL1344)
• Total number of polymer chains: 2
• Total formula weight: 28576.54

Authors

Pandey, N.K.,Ray, S.,Suar, M.,Bhavesh, N.S. (deposition date: 2016-03-08, release date: 2017-03-15, Last modification date: 2026-03-11)

Primary citation

Ray, S.,Pandey, N.K.,Kushwaha, G.S.,Das, S.,Ganguly, A.K.,Vashi, N.,Kumar, D.,Suar, M.,Bhavesh, N.S.
Structural investigation on SPI-6-associated Salmonella typhimurium VirG-like stress protein that promotes pathogen survival in macrophages.
Protein Sci., 31:835-849, 2022

PubMed Abstract: Enteric microbial pathogenesis, remarkably a complex process, is achieved by virulence factors encoded by genes located within regions of the bacterial genome termed pathogenicity islands. Salmonella pathogenicity islands (SPI) encodes proteins, that are essential virulence determinants for pathogen colonization and virulence. In addition to the well-characterized SPI-1 and SPI-2 proteins, which are required for bacterial invasion and intracellular replication, respectively, SPI-6 (formerly known as Salmonella enterica centisome 7 island [SCI]) encoding proteins are also known to play pivotal role in Salmonella pathogenesis. However, the underlying molecular mechanism of these proteins remained elusive. To gain molecular insights into SPI-6-associated proteins, in this study, a SPI-6 Salmonella typhimurium VirG-like protein (STV) is characterized using interdisciplinary experimental approaches including X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and infection assays. The high-resolution crystal structure, determined by the single-wavelength anomalous dispersion (SAD) method, reveals that STV belongs to the LTxxQ motif family. Solution-state NMR spectroscopy studies reveal that STV form a dimer involving interconnected helices. Interestingly, functional studies show that STV influence pathogen persistence inside macrophages in vitro at later stages of infection. Altogether, our findings suggest that STV, a member of the LTxxQ stress protein family, modulates bacterial survival mechanism in macrophages through SPI-1 and SPI-2 genes, respectively.

PubMed: 34997791
DOI: 10.1002/pro.4272

Experimental method

X-RAY DIFFRACTION (2.192 Å)