For the first time, an international team of scientists recreated in the lab the molecule that allows the tsetse fly to feed on blood. It’s a powerful yet small anticoagulant with a unique and strong binding to thrombin, the key enzyme of the coagulation pathway. X-ray diffraction measurements at two synchrotron facilities ––ALBA and ESRF–– were instrumental to understand the structure and the mechanism of action of this molecule, which suggests it is also a promising platform for designing improved anticoagulant drugs.
More than 170 participants from all Europe met up virtually for the third League of European Accelerator-based Photon Sources (LEAPS) Plenary meeting. The event has been hosted by the ALBA Synchrotron, whose director, Caterina Biscari, will continue as Chair of LEAPS in 2021.
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A study led by scientists from the XALOC beamline of the ALBA Synchrotron reports an in-depth structural analysis of bacterial proteins involved in conjugation: Rap and Rco, at various levels of atomic detail. They have demonstrated that Rap tetramerization is induced by peptide binding, through a novel “foot-2-foot” interaction, not previously seen in other proteins of the Rap family. Tetramerization hampers Rap-Rco interaction, releasing Rco, which is a repressor protein, and thereby blocking conjugation, the transfer of genetic material between bacteria.
LEAPS invited to a Zoom webinar on 28 October 2020, 10–12 CET "European Research Infrastructures: Engines for Science and Innovation" hosted by MEP and vice-chair of the ITRE Committee at the European Parliament, Lina Gálvez.
