ArticleJournal of molecular biology2009
Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of haemophilus influenzae immunoglobulin A1 protease.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 73 citations in OpenAlex.
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases.The EMBO journal · 2025Article
- The structure of the Gemella haemolysans M26 IgA1 protease trypsin-like domain.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Substitutions in the nonactive site of the passenger domain on the activity ofInfection and immunity · 2024Article
- Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function.Nature communications · 2023Article
- A substrate-induced gating mechanism is conserved among Gram-positive IgA1 metalloproteases.Communications biology · 2022Article
- Phylogenetic Classification and Functional Review of Autotransporters.Frontiers in immunology · 2022Review
- Structural and functional significance of the amino acid differences ValInternational journal of biological macromolecules · 2021Article
- Article
- Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021Article
- Mechanism and inhibition of Streptococcus pneumoniae IgA1 protease.Nature communications · 2020Article
- NBCZone: Universal three-dimensional construction of eleven amino acids near the catalytic nucleophile and base in the superfamily of (chymo)trypsin-like serine fold proteases.International journal of biological macromolecules · 2020Article
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- Small-Molecule Inhibitors ofACS infectious diseases · 2019Article
- Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.PloS one · 2018Article
- Streptococcus pneumoniae IgA1 protease: A metalloprotease that can catalyze in a split manner in vitro.Protein science : a publication of the Protein Society · 2017Article
- Subdomain 2 of the Autotransporter Pet Is the Ligand Site for Recognizing the Pet Receptor on the Epithelial Cell Surface.Infection and immunity · 2016Article
- Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.Molecular microbiology · 2015Review
- Role of class 1 serine protease autotransporter in the pathogenesis of Citrobacter rodentium colitis.Infection and immunity · 2014Article
- Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence.Cellular and molecular life sciences : CMLS · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We report here the first structure of a member of the immunoglobulin A protease (IgAP) family at 1.75-A resolution. This protease is a founding member of the type V (autotransporter) secretion system and is considered a virulence determinant among the bacteria expressing the enzyme. The structure of the enzyme fits that of a classic autotransporter in which several unique domains necessary for protein function are appended to a central, 100-A-long beta-helical domain. The N-terminal domain of the IgAP is found to possess a chymotrypsin-like fold. However, this catalytic domain contains a unique loop D that extends over the active site acting as a lid, gating substrate access. The data presented provide a structural basis for the known ability of IgAPs to cleave only the proline/serine/threonine-rich hinge peptide unique to IgA1 (isotype 1) in the context of the intact fold of the immunoglobulin. Based upon the structural data, as well as molecular modeling, a model suggesting that the unique extended loop D in this IgAP sterically occludes the active-site binding cleft in the absence of immunoglobulin binding is presented. Only in the context of binding of the IgA1-Fc domain in a valley formed between the N-terminal protease domain and another domain appended to the beta-helix spine (domain 2) is the lid stabilized in an open conformation. The stabilization of this open conformation through Fc association subsequently allows access of the hinge peptide to the active site, resulting in recognition and cleavage of the substrate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.