ArticleProceedings of the National Academy of Sciences of the United States of America2014
An intramolecular lock facilitates folding and stabilizes the tertiary structure of Streptococcus mutans adhesin P1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Phosphorylated lantibiotics-producing commensals integrate into the human oral microbiome to suppress pathogens and promote microbiome homeostasis.NPJ biofilms and microbiomes · 2026Article
- Backbone NMR resonance assignments for the C2 domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2025Article
- Virtual Screening of Inhibitors ofACS medicinal chemistry letters · 2024Article
- Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2023Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.AMB Express · 2021Article
- Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021Article
- Discovery of fibrillar adhesins across bacterial species.BMC genomics · 2021Article
- Function-adaptive clustered nanoparticles reverse Streptococcus mutans dental biofilm and maintain microbiota balance.Communications biology · 2021Article
- In Silico Selection and In Vitro Evaluation of New Molecules That Inhibit the Adhesion ofInternational journal of molecular sciences · 2020Article
- Characterization of an intermolecular quaternary interaction between discrete segments of the Streptococcus mutans adhesin P1 by NMR spectroscopy.The FEBS journal · 2020Article
- Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids.Scientific reports · 2020Article
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- The Role of Functional Amyloids in Bacterial Virulence.Journal of molecular biology · 2018Review
- Crystal structure of an anti-CRISPR protein, AcrIIA1.Nucleic acids research · 2018Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Streptococcus Mutans Adhesin Biotypes that Match and Predict Individual Caries Development.EBioMedicine · 2017Article
- K+ modulates genetic competence and the stress regulon of Streptococcus mutans.Microbiology (Reading, England) · 2017Article
- Functional amyloids in Streptococcus mutans, their use as targets of biofilm inhibition and initial characterization of SMU_63c.Microbiology (Reading, England) · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The cariogenic bacterium Streptococcus mutans uses adhesin P1 to adhere to tooth surfaces, extracellular matrix components, and other bacteria. A composite model of P1 based on partial crystal structures revealed an unusual complex architecture in which the protein forms an elongated hybrid alpha/polyproline type II helical stalk by folding back on itself to display a globular head at the apex and a globular C-terminal region at the base. The structure of P1's N terminus and the nature of its critical interaction with the C-terminal region remained unknown, however. We have cocrystallized a stable complex of recombinant N- and C-terminal fragments and here describe a previously unidentified topological fold in which these widely discontinuous domains are intimately associated. The structure reveals that the N terminus forms a stabilizing scaffold by wrapping behind the base of P1's elongated stalk and physically "locking" it into place. The structure is stabilized through a highly favorable ΔG(solvation) on complex formation, along with extensive hydrogen bonding. We confirm the functional relevance of this intramolecular interaction using differential scanning calorimetry and circular dichroism to show that disruption of the proper spacing of residues 989-1001 impedes folding and diminishes stability of the full-length molecule, including the stalk. Our findings clarify previously unexplained functional and antigenic properties of P1.
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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.