ArticleActa crystallographica. Section D, Biological crystallography2014
A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Asymmetric isopeptide bond steers directional genomic RNA egress from icosahedral virus.Science advances · 2025Article
- Accelerating the design of pili-enabled living materials using an integrative technological workflow.Nature chemical biology · 2024Article
- Rising prevalence and drug resistance ofFrontiers in cellular and infection microbiology · 2024Review
- LrpCBA pilus proteins of gut-dwelling Ligilactobacillus ruminis: crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Crystal structure of the atypically adhesive SpaB basal pilus subunit: Mechanistic insights about its incorporation in lactobacillar SpaCBA pili.Current research in structural biology · 2020Article
- Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.Scientific reports · 2019Article
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.International journal of molecular sciences · 2017Review
- Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability.Scientific reports · 2017Article
- Article
- Reduction of lattice disorder in protein crystals by high-pressure cryocooling.Journal of applied crystallography · 2016Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.Nature communications · 2015Article
- Purification, crystallization and preliminary X-ray diffraction analysis of SpaD, a backbone-pilin subunit encoded by the fimbrial spaFED operon in Lactobacillus rhamnosus GG.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Engineering of Metabolic Pathways by Artificial Enzyme Channels.Frontiers in bioengineering and biotechnology · 2015Review
- Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The Gram-positive organism Corynebacterium diphtheriae, the cause of diphtheria in humans, expresses pili on its surface which it uses for adhesion and colonization of its host. These pili are covalent protein polymers composed of three types of pilin subunit that are assembled by specific sortase enzymes. A structural analysis of the major pilin SpaD, which forms the polymeric backbone of one of the three types of pilus expressed by C. diphtheriae, is reported. Mass-spectral and crystallographic analysis shows that SpaD contains three internal Lys-Asn isopeptide bonds. One of these, shown by mass spectrometry to be located in the N-terminal D1 domain of the protein, only forms slowly, implying an energy barrier to bond formation. Two crystal structures, of the full-length three-domain protein at 2.5 Å resolution and of a two-domain (D2-D3) construct at 1.87 Å resolution, show that each of the three Ig-like domains contains a single Lys-Asn isopeptide-bond cross-link, assumed to give mechanical stability as in other such pili. Additional stabilizing features include a disulfide bond in the D3 domain and a calcium-binding loop in D2. The N-terminal D1 domain is more flexible than the others and, by analogy with other major pilins of this type, the slow formation of its isopeptide bond can be attributed to its location adjacent to the lysine used in sortase-mediated polymerization during pilus assembly.
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