scholarly journals Application of Radioisotopes in Biochemical Analyses: Metal Binding Proteins and Metal Transporters

10.5772/22130 ◽  
2011 ◽  
Author(s):  
Miki Kawachi ◽  
Nahoko Nagasaki-Takeuchi ◽  
Mariko Kato ◽  
Masayoshi Maeshim
Keyword(s):  
Metal Binding ◽  
Binding Proteins ◽  
Metal Transporters ◽  
Biochemical Analyses

Metal pollution assessment of the marine environment by determination of metal-binding proteins in Mytilus sp.

1987 ◽  
Vol 22 (2-4) ◽  
pp. 235-248 ◽  
Author(s):  
J Pavičič ◽  
M Škreblin ◽  
B Raspor ◽  
M Branica ◽  
M Tušek-Ẑnidarič ◽  
...  
Keyword(s):  
Marine Environment ◽  
Metal Pollution ◽  
Metal Binding ◽  
Binding Proteins ◽  
Pollution Assessment

scholarly journals Structural dissection of a complex Bacteroides ovatus gene locus conferring xyloglucan metabolism in the human gut

Open Biology ◽  
2016 ◽  
Vol 6 (7) ◽  
pp. 160142 ◽  
Author(s):  
Glyn R. Hemsworth ◽  
Andrew J. Thompson ◽  
Judith Stepper ◽  
Łukasz F. Sobala ◽  
Travis Coyle ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Bacterial Species ◽  
Three Dimensional ◽  
Human Gastrointestinal Tract ◽  
Human Gut ◽  
Molecular Machinery ◽  
Bacteroides Ovatus ◽  
Biochemical Analyses ◽  
Individual Specificity

The human gastrointestinal tract harbours myriad bacterial species, collectively termed the microbiota, that strongly influence human health. Symbiotic members of our microbiota play a pivotal role in the digestion of complex carbohydrates that are otherwise recalcitrant to assimilation. Indeed, the intrinsic human polysaccharide-degrading enzyme repertoire is limited to various starch-based substrates; more complex polysaccharides demand microbial degradation. Select Bacteroidetes are responsible for the degradation of the ubiquitous vegetable xyloglucans (XyGs), through the concerted action of cohorts of enzymes and glycan-binding proteins encoded by specific xyloglucan utilization loci (XyGULs). Extending recent (meta)genomic, transcriptomic and biochemical analyses, significant questions remain regarding the structural biology of the molecular machinery required for XyG saccharification. Here, we reveal the three-dimensional structures of an α-xylosidase, a β-glucosidase, and two α- l -arabinofuranosidases from the Bacteroides ovatus XyGUL. Aided by bespoke ligand synthesis, our analyses highlight key adaptations in these enzymes that confer individual specificity for xyloglucan side chains and dictate concerted, stepwise disassembly of xyloglucan oligosaccharides. In harness with our recent structural characterization of the vanguard endo-xyloglucanse and cell-surface glycan-binding proteins, the present analysis provides a near-complete structural view of xyloglucan recognition and catalysis by XyGUL proteins.

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