2ag7

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

STRUCTURAL MODEL OF SILICATEIN ALPHA FROM TETHYA AURANTIASTRUCTURAL MODEL OF SILICATEIN ALPHA FROM TETHYA AURANTIA

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Silicateins are proteins with catalytic, structure-directing activity that are responsible for silica biosynthesis in certain sponges; they are the constituents of macroscopic protein filaments that are found occluded within the silica needles made by Tethya aurantia. Self-assembly of the silicatein monomers and oligomers is shown to form fibrous structures by a mechanism that is fundamentally different from any previously described filament-assembly process. This assembly proceeds through the formation of diffusion-limited, fractally patterned aggregates on the path to filament formation. The driving force for this self-assembly is suggested to be entropic, mediated by the interaction of hydrophobic patches on the surfaces of the silicatein subunits that are not found on highly homologous congeners that do not form filaments. Our results are consistent with a model in which silicatein monomers associate into oligomers that are stabilized by intermolecular disulfide bonds. These oligomeric units assemble into a fractal network that subsequently condenses and organizes into a filamentous structure. These results represent a potentially general mechanism for protein fiber self-assembly. Fractal intermediates in the self-assembly of silicatein filaments.,Murr MM, Morse DE Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11657-62. Epub 2005 Aug 9. PMID:16091468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2ag7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image