A schematic representation of the membrane domain of E. coli NDH1... Download Scientific Diagram


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Enteropathogenic E. coli (EPEC) is an enteric pathogen estimated to cause 30-40% of all infantile diarrhoea in developing countries. 1 EPEC constitutes a significant health risk with a mortality rate of approximately one-third resulting in the death of several hundred thousand children each year. 1 Spread through the fecal/oral route, once ingested EPEC is able to take residence in the small.


A schematic representation of the membrane domain of E. coli NDH1... Download Scientific Diagram

Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Giang Thi Tuyet Nguyen1†, Aleksi Sutinen1†, Arne Raasakka2, Gopinath Muruganandam3,4, Remy Loris3 ,4 and Petri Kursula1 2* 1Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland, 2Department of


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Figure 4. Identification of key loops for EnvC binding in the EcoFtsEX/EnvC Complex. (A) Overlay of EcoFtsEX and EcoFtsEX/EnvC complexes, with a focus on the conformational changes in the PLD domain induced by EnvC binding.The overall overlay of EcoFtsEX and EcoFtsEX/EnvC is depicted in ribbon form.Color scheme: FtsE (magenta and dark green), FtsX (cornflower blue and rosy brown), Porter of.


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Background. Little information exists on the mobility of (integral) outer membrane proteins (OMPs) in the bacterial OM. Traditionally, the bacterial outer membrane is presented as a tight, gel-like barrier, with LPS packed together with cations in a crystalline matrix [1,2].At the same time, experimental evidence suggests that integral outer membrane protein IcsA is able to diffuse laterally.


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The yeast Pichia pastoris is a cost-effective and easily scalable system for recombinant protein production. In this work we compared the conformation of the receptor binding domain (RBD) from.


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The isomerase activity of the C-terminal fructose-6P binding domain (residues 241-608) of glucosamine-6-phosphate synthase from Escherichia coli has been studied.


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(A) In E. coli, dolP is located downstream of diaA and encodes a lipoprotein with a signal sequence (orange) and two BON domains (red). The signal sequence is cleaved by LspA, the cysteine at position 19 acylated by Lgt and Lnt and finally the protein is targeted to the OM by the Lol system ( Figure 1—figure supplement 1 ).


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Two plasmid vectors encoding the A and B subunits of cholera toxin (CT) and two additional vectors encoding the A and B subunits of the Escherichia coli heat-labile enterotoxin (LT) were evaluated for their ability to serve as genetic adjuvants for particle-mediated DNA vaccines administered to the epidermis of laboratory animals. Both the CT and the LT vectors strongly augmented Th1 cytokine.


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Fructose-6-phosphate Binding Domain of Glucosamine-6-phosphate Synthase from Escherichia coli ROUMIANA TODOROVA+ Znstitute of Biophysics, Bulgarian Academy of Sciences, 1113 Sofa, Bulgaria (Received 6 February 2001) The isomerase activity of the C-terminal fructose-6P binding domain (residues 241-608) of glucosamine- 6-phosphate synthase from.


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The 4.6 Mbp E. coli circular bacterial chromosome is organized about a transverse axis,. Assuming L3-R3 movement reflects in large part domain movement, we expect chromosome domain mobility on average to be 7- to 10-fold less than that of the replisome. We note that loci undergoing replication may exhibit different dynamics, although we.


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