Structure of metalloproteins, membrane proteins, filamentous sarcomer proteins, and virus particles

Our work focusses on biological nitrogen fixation by Nitrogenase, on metalloenzymes and integral membrane proteins of bacterial and archaeal respiratory systems (Andrade/Einsle/Wohlwend), the working mechanism and regulation of medically relevant membrane proteins and complexes and their defects leading to pathologies (Hunte/Wirth), bacterial antibiotic resistance factors and viral and bacterial proteins bound to their targets or inhibitors, and their interactions with glycans (Stehle/Zocher), human S100 proteins involved in nutritional immunity, USP18 enforcing the endogenous antiviral interferon response, and the respiratory complex NQR of V. cholerae (Fritz), DNA Polymerases with artificial substrates (Betz), and on multi-domain components of the sarcomeric filamentous protein titin and their binding to the E3 ubiquitin ligase MuRF1 and the central myosin rod-domain (Mayans).

本研究聚焦于以下多个研究方向：由固氮酶（Nitrogenase）介导的生物固氮，细菌与古菌呼吸系统中的金属酶及整合膜蛋白（Andrade/Einsle/Wohlwend团队）；医学相关膜蛋白及其复合物的工作机制与调控，以及其缺陷引发的病理变化（Hunte/Wirth团队）；细菌抗生素耐药因子、结合靶点或抑制剂的病毒与细菌蛋白，及其与聚糖（glycans）的相互作用（Stehle/Zocher团队）；参与营养免疫的人源S100蛋白、强化内源性抗病毒干扰素应答的USP18，以及霍乱弧菌（V. cholerae）呼吸复合物NQR（Fritz团队）；搭载人工底物的DNA聚合酶（DNA Polymerase，Betz团队）；肌节丝状蛋白肌联蛋白（titin）的多结构域组分，及其与E3泛素连接酶MuRF1和肌球蛋白中央杆状结构域的结合作用（Mayans团队）。