About the cover
May 2008 Volume 4 No 5
Mannosidase catalysis through an unusual boat-like transition state. Tailford et al. (p 306) solved the structure of 
-mannosidase bound to potent inhibitors and found that all bound in a B2,5 (boat) or closely related conformation. Biochemical analysis demonstrated that these inhibitors were acting as transition state mimics. Together these results provide the first direct evidence for a boat-like transition state in -mannosidases (see also News and Views by Palcic on p 269). Shown is the conformational map of pyranoid ring interconversion overlaid on the ceiling of a gazebo. Cover art by Erin Boyle based on chemical structures provided by Spencer Williams, Bruno Bernet and Andrea Vasella.
-mannosidase bound to potent inhibitors and found that all bound in a B2,5 (boat) or closely related conformation. Biochemical analysis demonstrated that these inhibitors were acting as transition state mimics. Together these results provide the first direct evidence for a boat-like transition state in -mannosidases (see also News and Views by Palcic on p 269). Shown is the conformational map of pyranoid ring interconversion overlaid on the ceiling of a gazebo. Cover art by Erin Boyle based on chemical structures provided by Spencer Williams, Bruno Bernet and Andrea Vasella. 