ArticleJournal of molecular biology2010
Two intramolecular isopeptide bonds are identified in the crystal structure of the Streptococcus gordonii SspB C-terminal domain.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 62 citations in OpenAlex.
- Cryo-EM structure of the native assembled Mfa type V pilus from the periodontal pathogen Porphyromonas gingivalis.Communications biology · 2026Article
- The structure ofInfection and immunity · 2026Article
- The genotypic characterization ofFrontiers in microbiology · 2025Article
- Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation, and virulence.eLife · 2023Article
- Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021Article
- Genetics, Structure, and Function of Group A Streptococcal Pili.Frontiers in microbiology · 2021Review
- Identification of Small-Molecule Inhibitors Targeting Porphyromonas gingivalis Interspecies Adherence and Determination of TheirAntimicrobial agents and chemotherapy · 2020Article
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 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
- Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.Scientific reports · 2019Article
- Aggregatibacter actinomycetemcomitans mediates protection of Porphyromonas gingivalis from Streptococcus sanguinis hydrogen peroxide production in multi-species biofilms.Scientific reports · 2019Article
- Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability.Scientific reports · 2017Article
- Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae.The Journal of biological chemistry · 2016Article
- Isopeptide bond in collagen- and fibrinogen-binding MSCRAMMs.Biophysical reviews · 2016Review
- A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Autocatalytically generated Thr-Gln ester bond cross-links stabilize the repetitive Ig-domain shaft of a bacterial cell surface adhesin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes.FEBS open bio · 2014Article
- A proposed mechanism for the interaction between the Candida albicans Als3 adhesin and streptococcal cell wall proteins.Frontiers in microbiology · 2014Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
Streptococcus gordonii is a primary colonizer and is involved in the formation of dental plaque. This bacterium expresses several surface proteins. One of them is the adhesin SspB, which is a member of the Antigen I/II family of proteins. SspB is a large multi-domain protein that has interactions with surface molecules on other bacteria and on host cells, and is thus a key factor in the formation of biofilms. Here, we report the crystal structure of a truncated form of the SspB C-terminal domain, solved by single-wavelength anomalous dispersion to 1.5 A resolution. The structure represents the first of a C-terminal domain from a streptococcal Antigen I/II protein and is comprised of two structurally related beta-sandwich domains, C2 and C3, both with a Ca(2+) bound in equivalent positions. In each of the domains, a covalent isopeptide bond is observed between a lysine and an asparagine, a feature that is believed to be a common stabilization mechanism in Gram-positive surface proteins. S. gordonii biofilms contain attachment sites for the periodontal pathogen Porphyromonas gingivalis and the SspB C-terminal domain has been shown to have one such recognition motif, the SspB adherence region. The motif protrudes from the protein, and serves as a handle for attachment. The structure suggests several additional putative binding surfaces, and other binding clefts may be created when the full-length protein is folded.
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