scholarly journals Biosynthesis and self-assembly of protein S, a development-specific protein of Myxococcus xanthus

1979 ◽  
Vol 76 (1) ◽  
pp. 209-213 ◽  
Author(s):  
M. Inouye ◽  
S. Inouye ◽  
D. R. Zusman
Keyword(s):  
Self Assembly ◽  
Myxococcus Xanthus ◽  
Protein S ◽  
Specific Protein

scholarly journals Effects of deletion of the gene for the development-specific protein S on differentiation in Myxococcus xanthus.

1984 ◽  
Vol 158 (3) ◽  
pp. 1195-1197 ◽  
Author(s):  
T Komano ◽  
T Furuichi ◽  
M Teintze ◽  
M Inouye ◽  
S Inouye
Keyword(s):  
Myxococcus Xanthus ◽  
Protein S ◽  
Specific Protein

scholarly journals Crystallization and preliminary X-ray analysis of the FliH–FliI complex responsible for bacterial flagellar type III protein export

2012 ◽  
Vol 68 (11) ◽  
pp. 1311-1314 ◽  
Author(s):  
Yumiko Uchida ◽  
Tohru Minamino ◽  
Keiichi Namba ◽  
Katsumi Imada
Keyword(s):  
Self Assembly ◽  
Specific Protein ◽  
Protein Export ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Peg 400 ◽  
Diffusion Technique ◽  
Flagellar Proteins ◽  
Soluble Components

The bacterial flagellar proteins are translocated into the central channel of the flagellum by a specific protein-export apparatus for self-assembly at the distal growing end. FliH and FliI are soluble components of the export apparatus and form an FliH2–FliI heterotrimer in the cytoplasm. FliI is an ATPase and the FliH2–FliI complex delivers export substrates from the cytoplasm to an export gate made up of six integral membrane proteins of the export apparatus. In this study, an FliHCfragment consisting of residues 99–235 was co-purified with FliI and the FliHC2–FliI complex was crystallized. Crystals were obtained using the hanging-drop vapour-diffusion technique with PEG 400 as a precipitant. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 133.7,b= 147.3,c= 164.2 Å, and diffracted to 3.0 Å resolution.

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