Johan P. Turkenburg

TL;DR: 3-D structure of the GH25 enzyme from Bacillus anthracis is reported, showing that the active center is extremely similar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration using the neighboring-group catalytic mechanism that is common to this 'super-family' of enzymes.

TL;DR: The rational design, synthesis, and characterization of human insulin analogues structurally locked in expected R- or T-states revealed that the T-like state is indeed important for the folding efficiency of (pro)insulin and that a substantial flexibility of the B1–B8 segment, where GlyB8 plays a key role, is a crucial prerequisite for an efficient insulin–IR interaction.

TL;DR: Although it shares the overall fold of cytochromes P450 of known structure, XplA-heme is unusual in that the kinked I-helix that traverses the distal face of the heme is broken by Met-394 and Ala-395, important in oxidative P450s for the scission of the dioxygen bond prior to substrate oxygenation.

TL;DR: Ion-pair reinforced, hydrogen-bonded molecular ribbons are knitted together through ammonium carboxylate salt bridges into undulating sheets wherein each component participates in three ion-pairing interactions and up to twelve hydrogen bonds.

TL;DR: Fibrinogen binding is sterically regulated by fibronectin binding, and this mechanism might result in targeting of S. aureus to fibrin-rich thrombi or elastin- rich tissues.