María Lucas

TL;DR: The recently described lytic polysaccharide monooxygenases have attracted the highest attention among copper oxidoreductases, since they are capable of oxidatively breaking down crystalline cellulose, the disintegration of which is still a major bottleneck in lignocellulose biorefineries, along with lignin degradation.

TL;DR: The results suggest that MR is an ATP-controlled transient molecular clamp at DNA double-strand breaks, a clamp conformation with increased DNA-binding activity.

TL;DR: An X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II identifies a binding site for canonical recycling signals at the interface between VPS 26 and SNX 3.

TL;DR: The three-dimensional structure of the relaxase domain of TrwC in complex with its cognate DNA at oriT shows a fold built on a two-layer α/β sandwich, with a deep narrow cleft that houses the active site.

TL;DR: It is established that the water hydrolysis takes place with an activation barrier of 30 kcal mol(-1), confirming the very slow reaction observed experimentally, and that the rate-limiting process is the first hydration, and ascertained the importance of a water molecule close to the two amine groups in lowering the activation barriers for the ring-opening reaction.