Joseph E. Wedekind

TL;DR: A superfamily of enzymes related by their ability to catalyze the abstraction of the alpha-proton of a carboxylic acid to form an enolic intermediate is discovered, and the established and deduced structure-function relationships in the superfamily allow the prediction that other apparent members of the family for which no catalytic functions have yet been assigned will also perform chemistry involving abstraction of their alpha-protons.

TL;DR: Several proteins have been identified as being similar to C-to-U mRNA editing enzymes based on their structural domains and the occurrence of a catalytic domain characteristic of cytidine deaminases and their structure, expression and relevance to biomedically significant processes or pathologies are considered.

TL;DR: A protein-ligand X-ray crystal structure of inhibitor 3-bound HIV-1 protease revealed extensive interactions in the HIV protease active site including strong hydrogen bonding interactions with the backbone, which may lead to novel inhibitors that can combat drug resistance.

TL;DR: The refined structures of exotoxin A provide precise models for the design and interpretation of further studies of the mechanism of intoxication and clarify several ionic interactions within structural domains I and II that may modulate an obligatory conformational change that is induced by low pH.

TL;DR: In this paper, the crystal structures of the preQ1 riboswitch from Thermo-anaerobacter tengcongensis were analyzed in both bound and free states, and it was shown that the ligand pocket shifts into the pre-Q1 binding site, resulting in closed access to the metabolite while simultaneously increasing exposure of the ribosome-binding site.