Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum

2012 ◽  
Vol 151 (6) ◽  
pp. 589-592 ◽  
Author(s):  
H. Shimizu ◽  
A. Osanai ◽  
K. Sakamoto ◽  
D. K. Inaoka ◽  
T. Shiba ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Parasitic Nematode ◽  
Ascaris Suum ◽  
Fumarate Reductase

Characterization of 5-HT receptors in the parasitic nematode, Ascaris suum

Parasitology ◽  
2001 ◽  
Vol 122 (02) ◽  
Author(s):  
J.E. TRIM ◽  
L. HOLDEN-DYE ◽  
J. WILLSON ◽  
M. LOCKYER ◽  
R.J. WALKER
Keyword(s):  
Parasitic Nematode ◽  
Ascaris Suum

The ABA-1 Allergen of the Parasitic Nematode Ascaris suum: Fatty Acid and Retinoid Binding Function and Structural Characterization

Biochemistry ◽  
1995 ◽  
Vol 34 (20) ◽  
pp. 6700-6710 ◽  
Author(s):  
Malcolm W. Kennedy ◽  
Andrew Brass ◽  
Alan B. McCruden ◽  
Nicholas C. Price ◽  
Sharon M. Kelly ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Structural Characterization ◽  
Parasitic Nematode ◽  
Ascaris Suum ◽  
Binding Function

An ion-sensitive microelectrode study on the effect of a high concentration of ivermectin on chloride balance in the somatic muscle bag cells of Ascaris suum

Parasitology ◽  
1993 ◽  
Vol 106 (4) ◽  
pp. 421-427 ◽  
Author(s):  
H. R. Parri ◽  
M. B. A. Djamgoz ◽  
L. Holden-Dye ◽  
R. J. Walker
Keyword(s):  
Receptor Antagonist ◽  
Chloride Channel ◽  
Gaba Receptor ◽  
Parasitic Nematode ◽  
Ascaris Suum ◽  
Muscle Cells ◽  
High Concentration ◽  
Somatic Muscle ◽  
Ion Sensitive Microelectrodes ◽  
Bag Cells

SUMMARYIvermectin has been shown to increase chloride conductances of invertebrate cells. On the muscle cells of the parasitic nematode Ascaris, ivermectin acts as both a GABA receptor antagonist and a chloride channel opener. In this study, ion-sensitive microelectrodes were used to investigate the effect of ivermectin on intracellular C1− concentration of the somatic muscle bag cells of Ascaris suum. Incubation of muscle cells with ivermectin (10 μM in 1% dimethyl sulphoxide vehicle for 60 min) increased intracellular C1− by 2·9 mM or 15% compared to controls (P > 0·01, n = 6).

scholarly journals Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1

Crystals ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 504 ◽  
Author(s):  
Kim ◽  
Kwon ◽  
Jung ◽  
Chun ◽  
Ha ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Flavin Adenine Dinucleotide ◽  
Structural Information ◽  
Redox Balance ◽  
Underlying Mechanism ◽  
Fumarate Reductase ◽  
Mutant Form ◽  
Characteristic Features ◽  
Fad Binding

Soluble fumarate reductase is essential for survival under anaerobic conditions. This enzyme can maintain the redox balance in the cell by catalyzing the reduction of fumarate to succinate. Although the overall reaction mechanism of soluble fumarate reductase in yeast, Osm1, has been proposed by a previous structural study, the details of the underlying mechanism are not completely elucidated. The present study provides the structural information regarding the active site mutant form of Osm1 (R326A), thus, revealing that R326A mutation does not affect the substrate binding. Structural alterations of the residues surrounding the active site, and the missing 2nd flavin adenine dinucleotide (FAD) in the previously defined 2nd FAD binding site, were observed as characteristic features of the Osm1 R326A crystal structure. Based on these findings, we provided a clue that can explain the loss of activity of Osm1 R326A.

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