ArticleBiochimica et biophysica acta2011
The prediction and characterization of YshA, an unknown outer-membrane protein from Salmonella typhimurium.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- Role of OB-Fold Protein YdeI in Stress Response and Virulence of Salmonella enterica Serovar Enteritidis.Journal of bacteriology · 2020Article
- EpitoCore: Mining Conserved Epitope Vaccine Candidates in the Core Proteome of Multiple Bacteria Strains.Frontiers in immunology · 2020Article
- High-resolution structure prediction ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- A novel transport mechanism for MOMP in Chlamydophila pneumoniae and its putative role in immune-therapy.PloS one · 2013Article
- TMBB-DB: a transmembrane β-barrel proteome database.Bioinformatics (Oxford, England) · 2012Article
- An adhesion protein of Salmonella enterica serovar Typhi is required for pathogenesis and potential target for vaccine development.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
We have developed an effective pathway for the prediction and characterization of novel transmembrane β-barrel proteins. The Freeman-Wimley algorithm, which is a highly accurate prediction method based on the physicochemical properties of experimentally characterized transmembrane β barrel (TMBB) structures, was used to predict TMBBs in the genome of Salmonella typhimurium LT2. The previously uncharacterized product of gene yshA was tested as a model for validating the algorithm. YshA is a highly conserved 230-residue protein that is predicted to have 10 transmembrane β-strands and an N-terminal signal sequence. All of the physicochemical and spectroscopic properties exhibited by YshA are consistent with the prediction that it is a TMBB. Specifically, recombinant YshA localizes to the outer membrane when expressed in Escherichia coli; YshA has a β-sheet-rich secondary structure with stable tertiary contacts in the presence of detergent micelles or when reconstituted into a lipid bilayer. When in a lipid bilayer, YshA forms a membrane-spanning pore with an effective radius of ~0.7nm. Taken together, these data substantiate the predictions made by the Freeman-Wimley algorithm by showing that YshA is a TMBB protein.
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