ArticleJournal of molecular biology2011
Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- The crystal structure of the toxin EspC from enteropathogenicGut microbes · 2025Article
- SPATEs promote the survival ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function.Nature communications · 2023Article
- Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms.NPJ biofilms and microbiomes · 2022Article
- Article
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Epithelial WNT2B and Desert Hedgehog Are Necessary for Human Colonoid Regeneration after Bacterial Cytotoxin Injury.iScience · 2020Article
- Serine Protease Autotransporters of theMicroorganisms · 2019Review
- Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.Nature communications · 2019Article
- Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin.PloS one · 2019Article
- Molecular basis for the folding of β-helical autotransporter passenger domains.Nature communications · 2018Article
- Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a β-Helical Passenger.Frontiers in microbiology · 2017Article
- An Acinetobacter trimeric autotransporter adhesin reaped from cells exhibits its nonspecific stickiness via a highly stable 3D structure.Scientific reports · 2016Article
- Article
- Determinants of Proteolysis and Cell-Binding for the Shigella flexneri Cytotoxin, SigA.Current microbiology · 2015Article
- Structure, Function, and Assembly of Adhesive Organelles by Uropathogenic Bacteria.Microbiology spectrum · 2015Review
- Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Molecular microbiology · 2015Review
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- Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal "passenger domain" responsible for the specific effector functions of the molecule and a C-terminal "β-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-Å crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel β-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this β-helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the β-helix within SPATEs.
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