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Samatey/3
From Proteopedia
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In actuality, the hook is assembled by the flagellar basal body, not in a vacuum. Hook monomers are believed to be secreted through a central channel in the basal body prior to assembly, as shown in a movie available at [[Flagella, bacterial|Bacterial Flagella]]. | In actuality, the hook is assembled by the flagellar basal body, not in a vacuum. Hook monomers are believed to be secreted through a central channel in the basal body prior to assembly, as shown in a movie available at [[Flagella, bacterial|Bacterial Flagella]]. | ||
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| + | ==Caulobacter Hook Model== | ||
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| + | A model of the hook of ''Caulobacter crecentus'' was made by manually docking the crystallographic structure of FlgE-Cc32 domains D2 and D3 into the 20 Å electron density map published in 1981<ref>PMID: 7338902</ref>. Here you can <scene name='47/478822/Caucr-hook-cao/1'>view this hook model</scene> (alpha carbons only, spacefilled to 3.5 Å<ref>The ''Caulobacter crecentus'' hook model contains 55 copies of the monomer, for a total of 121,055 non-hydrogen atoms. There are 16,665 alpha carbon atoms in the model. The van der Waals radius of carbon is 1.7 Å. In order to make the FlgE domains look solid, the alpha carbons are displayed with a radius of 3.5 Å.</ref>). | ||
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| + | Most of the large cavity is filled by domains D0 and D1, but these domains are missing in this model. | ||
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| + | Each of the 11 protofilaments has a distinct color, so there are 11 colors. Here, <scene name='47/478822/Caucr-hook-cao/2'>one protofilament is marked with a black line</scene>. Each protofilament forms one of the 11-start helices. | ||
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| + | There is a large space between domains D2+D3 '''within''' a protofilament. Thus, protofilaments are held together by interactions between D0 and D1 (missing in this model). However, domains D2+D3 interact '''between''' protofilaments, forming 6 helices. Here, <scene name='47/478822/Caucr-hook-cao/3'>one of the 6-start helices is marked with a red line, and the 6 starts are numbered</scene>. | ||
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<hr> | <hr> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 18:17, 19 October 2016
Interactive 3D Complement in Proteopedia
Scientific Reports an online, open access journal: nature.com/srep
Structural insights into bacterial flagellar hook similarities and specifities.
Young-Ho Yoon, Clive S. Barker, Paula V. Bulieris, Hideyuki Matsunami, and Fadel A. Samatey.
Scientific Reports 6:35552, 2016: nature.com/articles/srep35552. (DOI: 10.1038/srep35552)
The interactive Molecular Tour below assumes that you are familiar with the journal article.
Molecular Tour
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Notes and References
- ↑ Kido Y, Yoon YH, Samatey FA. Crystallization of a 79 kDa fragment of the hook protein FlgE from Campylobacter jejuni. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt, 12):1653-7. Epub 2011 Nov 30. PMID:22139190 doi:10.1107/S1744309111043272
- ↑ Wagenknecht T, DeRosier D, Shapiro L, Weissborn A. Three-dimensional reconstruction of the flagellar hook from Caulobacter crescentus. J Mol Biol. 1981 Sep 25;151(3):439-65. PMID:7338902 doi:http://dx.doi.org/10.1016/0022-2836(81)90005-X
- ↑ The Caulobacter crecentus hook model contains 55 copies of the monomer, for a total of 121,055 non-hydrogen atoms. There are 16,665 alpha carbon atoms in the model. The van der Waals radius of carbon is 1.7 Å. In order to make the FlgE domains look solid, the alpha carbons are displayed with a radius of 3.5 Å.
