The Bacterial Flagellar Hook: Difference between revisions
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==Structure of the Hook Monomer, FlgE== | ==Structure of the Hook Monomer, FlgE== | ||
<applet load='1wlg' size='300' frame='true' align='right' scene='The_Bacterial_Flagellar_Hook/1wlg_1_mmol/ | <applet load='1wlg' size='300' frame='true' align='right' scene='The_Bacterial_Flagellar_Hook/1wlg_1_mmol/2'/> | ||
The hook is composed of about 120 copies of the protein chain FlgE (the product of the [http://ecoliwiki.net/colipedia/index.php/flgE:Quickview gene flgE]). In 2004, Samatey ''et al.'' solved the structure of the mid-portion of the wild-type FlgE of ''Salmonella typhimurium'' by [[X-ray crystallography]] at a [[Resolution|resolution]] of 1.8 Å ([[1wlg]])<ref name="hook1">PMID: 15510139</ref>. FlgE has 402 amino acids. The fragment successfully crystallized, designated FlgE31, consisted of amino acids 71-369, of which 71-363 were resolved (72% of the full-length protein). Removal of the ends of the full-length chain (domain D0, see below) was required in order to coax the protein to crystallize, instead of forming filaments. | The hook is composed of about 120 copies of the protein chain FlgE (the product of the [http://ecoliwiki.net/colipedia/index.php/flgE:Quickview gene flgE]). In 2004, Samatey ''et al.'' solved the structure of the mid-portion of the wild-type FlgE of ''Salmonella typhimurium'' by [[X-ray crystallography]] at a [[Resolution|resolution]] of 1.8 Å ([[1wlg]])<ref name="hook1">PMID: 15510139</ref>. FlgE has 402 amino acids. The fragment successfully crystallized, designated FlgE31, consisted of amino acids 71-369, of which 71-363 were resolved (72% of the full-length protein). Removal of the ends of the full-length chain (domain D0, see below) was required in order to coax the protein to crystallize, instead of forming filaments. | ||
FlgE consists of three domains, D0, D1, and D2. The (<scene name='The_Bacterial_Flagellar_Hook/1wlg_1_mmol/ | FlgE consists of three domains, D0, D1, and D2. The (<scene name='The_Bacterial_Flagellar_Hook/1wlg_1_mmol/2'>initial scene</scene>) at right shows D1 and D2 (D0 having been deleted in order to achieve crystallization, as mentioned above). | ||
{{Template:ColorKey_Amino2CarboxyRainbow}} | {{Template:ColorKey_Amino2CarboxyRainbow}} | ||
Note that D2 consists of a continuous segment of the protein chain, while D1 is made up of discontinuous segments. D0 (not shown, see above) is attached to D1, and D0 forms the inner channel of the hook. D2 forms the outer surface of the hook. | Note that D2 consists of a continuous segment of the protein chain, while D1 is made up of discontinuous segments. D0 (not shown, see above) is attached to D1, and D0 forms the inner channel of the hook. D2 forms the outer surface of the hook. | ||
Revision as of 11:18, 8 June 2009
The bacterial flagellar hook described in this article is one part of the bacterial flagellum. Please see Flagella, bacterial (under development at Sandbox4 Eric Martz) for an overview of where the hook fits in the flagellum.
The flagellar hook is a molecular universal joint that transmits torque from the motor, anchored in the bacterial cell wall, to the flagellar filament, the relatively rigid helical rod that propels the bacterial cell when rotated. The hook is flexible: it enables the filament to adopt a wide range of angles relative to the motor axis and cell wall, yet continue to be rotated by the motor at all these angles.
Structure of the Hook Monomer, FlgEStructure of the Hook Monomer, FlgE
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The hook is composed of about 120 copies of the protein chain FlgE (the product of the gene flgE). In 2004, Samatey et al. solved the structure of the mid-portion of the wild-type FlgE of Salmonella typhimurium by X-ray crystallography at a resolution of 1.8 Å (1wlg)[1]. FlgE has 402 amino acids. The fragment successfully crystallized, designated FlgE31, consisted of amino acids 71-369, of which 71-363 were resolved (72% of the full-length protein). Removal of the ends of the full-length chain (domain D0, see below) was required in order to coax the protein to crystallize, instead of forming filaments.
FlgE consists of three domains, D0, D1, and D2. The () at right shows D1 and D2 (D0 having been deleted in order to achieve crystallization, as mentioned above).
| Amino Terminus | Carboxy Terminus |
Note that D2 consists of a continuous segment of the protein chain, while D1 is made up of discontinuous segments. D0 (not shown, see above) is attached to D1, and D0 forms the inner channel of the hook. D2 forms the outer surface of the hook.
(TO BE CONTINUED: Eric Martz 15:13, 6 June 2009 (IDT))(TO BE CONTINUED: Eric Martz 15:13, 6 June 2009 (IDT))
Content AttributionContent Attribution
The initial content for this article was adapted, with permission, from The Bacterial Flagellar Hook: A Molecular Universal Joint, authored by User:Eric Martz in 2004-2006 for Protein Explorer.
References and NotesReferences and Notes
- ↑ Samatey FA, Matsunami H, Imada K, Nagashima S, Shaikh TR, Thomas DR, Chen JZ, Derosier DJ, Kitao A, Namba K. Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature. 2004 Oct 28;431(7012):1062-8. PMID:15510139 doi:http://dx.doi.org/10.1038/nature02997