2ag7: Difference between revisions
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<StructureSection load='2ag7' size='340' side='right'caption='[[2ag7]]' scene=''> | <StructureSection load='2ag7' size='340' side='right'caption='[[2ag7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AG7 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ag7 FirstGlance], [https://www.ebi.ac.uk/pdbsum/2ag7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ag7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Latest revision as of 17:40, 17 November 2021
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STRUCTURAL MODEL OF SILICATEIN ALPHA FROM TETHYA AURANTIASTRUCTURAL MODEL OF SILICATEIN ALPHA FROM TETHYA AURANTIA
Structural highlights
Publication Abstract from PubMedSilicateins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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