ArticleThe Journal of biological chemistry2009
Structural and functional studies of truncated hemolysin A from Proteus mirabilis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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22 citing papers in PubMed, 38 citations in OpenAlex.
- Review
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- Structural and biophysical characterization of the secreted, β-helical adhesin EtpA of Enterotoxigenic Escherichia coli.PloS one · 2023Article
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- Comparative bioinformatic and proteomic approaches to evaluate the outer membrane proteome of the fish pathogen Yersinia ruckeri.Journal of proteomics · 2019Article
- Review
- Pathogenesis ofEcoSal Plus · 2018Review
- Review
- Proteolysis of truncated hemolysin A yields a stable dimerization interface.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.Nature communications · 2016Article
- Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Protein science : a publication of the Protein Society · 2015Article
- Proteus mirabilis and Urinary Tract Infections.Microbiology spectrum · 2015Review
- Structural determinants of the interaction between the TpsA and TpsB proteins in the Haemophilus influenzae HMW1 two-partner secretion system.Journal of bacteriology · 2015Article
- Structure of the secretion domain of HxuA from Haemophilus influenzae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- System specificity of the TpsB transporters of coexpressed two-partner secretion systems of Neisseria meningitidis.Journal of bacteriology · 2013Article
- Sequential unfolding of beta helical protein by single-molecule atomic force microscopy.PloS one · 2013Article
Corrections and comments
- Erratum issuedSmith, Joshua A [added]
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
In this study we analyzed the structure and function of a truncated form of hemolysin A (HpmA265) from Proteus mirabilis using a series of functional and structural studies. Hemolysin A belongs to the two-partner secretion pathway. The two-partner secretion pathway has been identified as the most common protein secretion pathway among Gram-negative bacteria. Currently, the mechanism of action for the two-partner hemolysin members is not fully understood. In this study, hemolysis experiments revealed a unidirectional, cooperative, biphasic activity profile after full-length, inactive hemolysin A was seeded with truncated hemolysin A. We also solved the first x-ray structure of a TpsA hemolysin. The truncated hemolysin A formed a right-handed parallel beta-helix with three adjoining segments of anti-parallel beta-sheet. A CXXC disulfide bond, four buried solvent molecules, and a carboxyamide ladder were all located at the third complete beta-helix coil. Replacement of the CXXC motif led to decreased activity and stability according to hemolysis and CD studies. Furthermore, the crystal structure revealed a sterically compatible, dry dimeric interface formed via anti-parallel beta-sheet interactions between neighboring beta-helix monomers. Laser scanning confocal microscopy further supported the unidirectional interconversion of full-length hemolysin A. From these results, a model has been proposed, where cooperative, beta-strand interactions between HpmA265 and neighboring full-length hemolysin A molecules, facilitated in part by the highly conserved CXXC pattern, account for the template-assisted hemolysis.
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