Maarten R. Egmond

TL;DR: In this paper, the authors introduced the concept of stabilized subtilisin proteases, wherein one or more prolines is substituted for a native amino acid at stabilizing positions defined both by the range of the dihedral angles in the primary structure present at the substitution site and by selected characteristics of the protease secondary structure in the vicinity of the substitution sites.

TL;DR: The crystal structure of OmpT from Escherichia coli is presented, which shows a 10‐stranded antiparallel β‐barrel that protrudes far from the lipid bilayer into the extracellular space and a novel proteolytic mechanism, involving a His-Asp dyad and an Asp—Asp couple that activate a putative nucleophilic water molecule.

TL;DR: The first crystal structure of a bacterial lipase, from Pseudomonas glumae, is reported, formed from three domains, the largest of which contains a subset of the α/β hydrolase fold and a calcium site.

TL;DR: X-ray structures of monomeric and dimeric OMPLA from E. coli provide a detailed view of activation by dimerization of a membrane protein.

TL;DR: Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance.