scholarly journals Endolysins of Bacillus anthracis Bacteriophages Recognize Unique Carbohydrate Epitopes of Vegetative Cell Wall Polysaccharides with High Affinity and Selectivity

2012 ◽  
Vol 134 (37) ◽  
pp. 15556-15562 ◽  
Author(s):  
Kai-For Mo ◽  
Xiuru Li ◽  
Huiqing Li ◽  
Lieh Yoon Low ◽  
Conrad P. Quinn ◽  
...  
Author(s):  
Ashley Law ◽  
Alexander Stergioulis ◽  
Andrei S. Halavaty ◽  
George Minasov ◽  
Wayne F. Anderson ◽  
...  

Bacillus anthracis is the causative agent of the deadly disease Anthrax. Its use in bioterrorism and its ability to re-emerge have brought renewed interest in this organism. B. anthracis is a Gram-positive bacterium that adds L-rhamnose to its cell-wall polysaccharides using the activated donor dTDP-β-L-rhamnose. The enzymes involved in the biosynthesis of the activated donor are absent in humans, which make them ideal targets for therapeutic development to combat pathogens. Here, the 2.65 Å resolution crystal structure of the fourth enzyme in the dTDP-β-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-β-L-rhamnose reductase (RfbD), is presented in complex with NADP+. This enzyme catalyzes the reduction of dTDP-4-dehydro-β-L-rhamnose to dTDP-β-L-rhamnose. Although the protein was co-crystallized in the presence of Mg2+, the protein lacks the conserved residues that coordinate Mg2+.


Crop Science ◽  
2003 ◽  
Vol 43 (2) ◽  
pp. 571 ◽  
Author(s):  
S. K. Stombaugh ◽  
J. H. Orf ◽  
H. G. Jung ◽  
D. A. Somers

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