Fadel A. Samatey Group: Difference between revisions
No edit summary |
Eric Martz (talk | contribs) No edit summary |
||
| (13 intermediate revisions by one other user not shown) | |||
| Line 1: | Line 1: | ||
:[[Fadel_A._Samatey_Group_%28Japanese%29|サマテイ研 (日本語) Fadel A. Samatey Group (Japanese)]][[ja:Fadel A. Samatey Group (Japanese)]] | :[[Fadel_A._Samatey_Group_%28Japanese%29|サマテイ研 (日本語) Fadel A. Samatey Group (Japanese)]][[ja:Fadel A. Samatey Group (Japanese)]] | ||
<table align="right" width="260" ><tr><td rowspan="2"> </td><td>[[Image:Flagellar hook em density 1ucu.jpg]]</td></tr><tr><td><font color="#00908c">Crystal structure of flagellar hook</font> fitted into <font color="magenta">electron density map</font> obtained by electron | <table align="right" width="260" ><tr><td rowspan="2"> </td><td>[[Image:Flagellar hook em density 1ucu.jpg]]</td></tr><tr><td><font color="#00908c">Crystal structure of flagellar hook</font> fitted into <font color="magenta">electron density map</font> obtained by cryo-electron microscopy<ref name="hook1">PMID:15510139</ref>.</td></tr></table> | ||
[[User:Fadel A. Samatey|Fadel A. Samatey]] | [[User:Fadel A. Samatey|Fadel A. Samatey]] was Head of the Transmembrane Trafficking Unit at the [http://www.oist.jp Okinawa Institute of Science and Technology (OIST)] (Japan), 2007-2016. Samatey's group uses [[X-ray crystallography]], cryo-Electron microscopy, genetic, and biochemical approaches to elucidate the structures and functions of proteins, especially type III secretion proteins in [[Flagella, bacterial|bacterial flagella]]. | ||
From 1996-2007 Samatey was a member of the Keiichi Namba Group, from 1996 at Matsushita Electric, from 1997 in the [http://www.fbs.osaka-u.ac.jp/labs/namba/npn/index.html ERATO Protonic Nanomachine Project], and from 2002 at [http://www.fbs.osaka-u.ac.jp/eng/labo/09a.html Osaka University], Japan. Samatey earned his Ph.D. in 1992 at [http://www.ujf-grenoble.fr/ Université Joseph Fourier] in Grenoble, France. | From 1996-2007 Samatey was a member of the Keiichi Namba Group, from 1996 at Matsushita Electric, from 1997 in the [http://www.fbs.osaka-u.ac.jp/labs/namba/npn/index.html ERATO Protonic Nanomachine Project], and from 2002 at [http://www.fbs.osaka-u.ac.jp/eng/labo/09a.html Osaka University], Japan. Samatey earned his Ph.D. in 1992 at [http://www.ujf-grenoble.fr/ Université Joseph Fourier] in Grenoble, France. | ||
[[#Contributions from OIST|Below]] are listed contributions from the Samatey Group, most recent first | [[#Contributions from OIST|Below]] are listed contributions from the Samatey Group, most recent first. | ||
==Interests and Objectives== | ==Interests and Objectives== | ||
| Line 17: | Line 17: | ||
==Contributions from 2011 to Present== | ==Contributions from 2011 to Present== | ||
<ref group="xtra">PMID: 29147015</ref><references group="xtra" /> | |||
<ref group="xtra">PMID: 29105867</ref><references group="xtra" /> | |||
<ref group="xtra">PMID: 29078764</ref><references group="xtra" /> | |||
:<table style="background: #d0ffd0;padding: 6px;"><tr><td>The “ID-Rod-Stretch” is an intrinsically disordered linker found in both FlgE and FlgG, the proteins that respectively make the hook and the distal rod of the bacterial flagellum. Experiments done in FlgE of ''Salmonella enterica'' and of ''Campylobacter jejuni'' reveal the role of the ID-Rod-Stretch in the formation and stability of the flagellar hook. [https://www.youtube.com/watch?v=ZUAdpWCQD_0 See the special video abstract.] [[User:Fadel A. Samatey/FlgE III/Intrinsically Disordered Flagellar Rod Stretch| See results in interactive 3D]]. </td></tr></table> | |||
<ref group="xtra">PMID: 27811912</ref><references group="xtra" /> | <ref group="xtra">PMID: 27811912</ref><references group="xtra" /> | ||
:<table style="background: #d0ffd0;padding: 6px;"><tr><td>The bacterial flagellar hook, which is made by the polymerization of multiple copies of FlgE protein, is a flexible segment connecting the flagellar filament to the motor. The structure presented in this article puts in evidence the complex web of interactions between FlgE molecules. These interactions stabilize the flagellar hook during its function as a universal joint.[[User:Fadel A. Samatey/FlgE II/Complete Flagellar Hook Structure| See results in interactive 3D]]. </td></tr></table> | |||
<ref group="xtra">PMID: 27759043</ref><references group="xtra" /> | <ref group="xtra">PMID: 27759043</ref><references group="xtra" /> | ||
:<table style="background: #d0ffd0;padding: 6px;"><tr><td>The assembly of about a hundred molecules of FlgE protein makes the bacterial flagellar hook. FlgE has a high variability in amino acid residues composition and in molecular weight. Our study shows that FlgE can be divided in two distinct parts. The first part comprises domains that are found in all FlgE proteins and will make the basic structure of the hook common to all flagellated bacteria. The second part, hyper-variable both in size and structure, will be bacteria dependent and will give to the hook additional and specific properties to the bacterium its belong to.[[User:Fadel A. Samatey/FlgE I| See results in interactive 3D]]. </td></tr></table> | |||
| Line 81: | Line 93: | ||
<ref group="xtra">PMID: 21301106</ref><references group="xtra" /> | <ref group="xtra">PMID: 21301106</ref><references group="xtra" /> | ||
==Contributions from 2001 to 2010== | ==Contributions from 2001 to 2010== | ||