ArticleActa crystallographica. Section D, Biological crystallography2012
Structure of the catalytic domain of the Salmonella virulence factor SseI.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Salmonella Typhimurium effector SseI inhibits chemotaxis and increases host cell survival by deamidation of heterotrimeric Gi proteins.PLoS pathogens · 2018Article
- CNF1-like deamidase domains: common Lego bricks among cancer-promoting immunomodulatory bacterial virulence factors.Pathogens and disease · 2018Review
- The Salmonella Effector SpvD Is a Cysteine Hydrolase with a Serovar-specific Polymorphism Influencing Catalytic Activity, Suppression of Immune Responses, and Bacterial Virulence.The Journal of biological chemistry · 2016Article
- A common assembly module in injectisome and flagellar type III secretion sorting platforms.Nature communications · 2015Article
- Crystal structure of human protein N-terminal glutamine amidohydrolase, an initial component of the N-end rule pathway.PloS one · 2014Article
- A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.Nature structural & molecular biology · 2013Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells.
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Registered trials
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