ArticleProceedings of the National Academy of Sciences of the United States of America2020
Natural hybrid silica/protein superstructure at atomic resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Co-option of Lysosomal Machinery for Sponge Biosilicification.bioRxiv : the preprint server for biology · 2026Article
- Molecular tuning of DNA framework-programmed silicification by cationic silica cluster attachment.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Honeycomb Biosilica in Sponges: From Understanding Principles of Unique Hierarchical Organization to Assessing Biomimetic Potential.Biomimetics (Basel, Switzerland) · 2023Article
- The genome of the reef-building glass spongeRoyal Society open science · 2023Article
- Arrested in Glass: Actin within Sophisticated Architectures of Biosilica in Sponges.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Inorganic Polymeric Materials for Injured Tissue Repair: Biocatalytic Formation and Exploitation.Biomedicines · 2022Review
- Insights into the structure and morphogenesis of the giant basal spicule of the glass sponge Monorhaphis chuni.Frontiers in zoology · 2021Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of highly symmetric skeletal elements in demosponges, called spicules, follows a unique biomineralization mechanism in which polycondensation of an inherently disordered amorphous silica is guided by a highly ordered proteinaceous scaffold, the axial filament. The enzymatically active proteins, silicateins, are assembled into a slender hybrid silica/protein crystalline superstructure that directs the morphogenesis of the spicules. Furthermore, silicateins are known to catalyze the formation of a large variety of other technologically relevant organic and inorganic materials. However, despite the biological and biotechnological importance of this macromolecule, its tertiary structure was never determined. Here we report the atomic structure of silicatein and the entire mineral/organic hybrid assembly with a resolution of 2.4 Å. In this work, the serial X-ray crystallography method was successfully adopted to probe the 2-µm-thick filaments in situ, being embedded inside the skeletal elements. In combination with imaging and chemical analysis using high-resolution transmission electron microscopy, we provide detailed information on the enzymatic activity of silicatein, its crystallization, and the emergence of a functional three-dimensional silica/protein superstructure in vivo. Ultimately, we describe a naturally occurring mineral/protein crystalline assembly at atomic resolution.
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