6ZQ3
Crystal Structure of Silicatein Alpha from Marine Sponge Tethya aurantium
Summary for 6ZQ3
| Entry DOI | 10.2210/pdb6zq3/pdb |
| Descriptor | Silicatein alpha (2 entities in total) |
| Functional Keywords | silica, silicatein, sponges, demosponges, spicules, hydrolase |
| Biological source | Tethya aurantium (Orange puffball sponge) |
| Total number of polymer chains | 1 |
| Total formula weight | 23292.54 |
| Authors | Goerlich, S.,Leonarski, R.J.,Tomizaki, T.,Zlotnikov, I. (deposition date: 2020-07-09, release date: 2020-12-02, Last modification date: 2024-10-16) |
| Primary citation | Gorlich, S.,Samuel, A.J.,Best, R.J.,Seidel, R.,Vacelet, J.,Leonarski, F.K.,Tomizaki, T.,Rellinghaus, B.,Pohl, D.,Zlotnikov, I. Natural hybrid silica/protein superstructure at atomic resolution. Proc.Natl.Acad.Sci.USA, 117:31088-31093, 2020 Cited by PubMed 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. PubMed: 33229574DOI: 10.1073/pnas.2019140117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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