Proteopedia:Featured JRN/1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(shorten the content)
(shorten the content)
Line 2: Line 2:
<tr><td>[[Image:Anim Samatey2 FigA I.gif]]</td></tr>
<tr><td>[[Image:Anim Samatey2 FigA I.gif]]</td></tr>
<tr><td><div class="scrolling">'''Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in ''Salmonella enterica''.'''<br>
<tr><td><div class="scrolling">'''Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in ''Salmonella enterica''.'''<br>
-
''H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey''. ''Scientific Reports'' '''6''':27399 2016 doi: [http://dx.doi.org/10.1038/srep27399 10.1038/srep27399]<br>
+
''H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey''. ''Scientific Reports'' 2016 doi: [http://dx.doi.org/10.1038/srep27399 10.1038/srep27399]<br>
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as ''Salmonella enterica'' or ''Escherichia coli''. Here we present the open and closed crystal structures of FlgA from ''Salmonella enterica serovar Typhimurium'', grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as ''Salmonella enterica'' or ''Escherichia coli''. Here we present the open and closed crystal structures of FlgA from ''Salmonella enterica serovar Typhimurium'', grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

Revision as of 19:04, 18 October 2018

Image:Anim Samatey2 FigA I.gif
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> Visit this I3DC complement >>>

Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky, Angel Herraez

Retrieved from "http://52.214.119.220/wiki/index.php/Proteopedia:Featured_JRN/1"
Personal tools