Dear All, I will be on a parental leave from 01/02/2022 until 31/01/2024. I will be following the scientific part of my job anyway and acting as a tutor for my PhD students from remote
Author: Stefano Benini
Stefano Benini 2009- Assistant Professor at the Free University of Bolzano 2007-2009 Protein crystallographer in the pharmaceutical company AstraZeneca plc., United Kingdom 2002-2007 Post Doc, York Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom 2000-2002 Post Doc, International Centre for Genetic Engineering and Biotechnology (ICGEB) Trieste, Italy 1996-2000 PhD student, European Molecular Biology Laboratory (EMBL) Hamburg (Germany) 1992-1996 Msc research assistant, Istituto di Chimica Agraria, Università di Bologna, Bologna, Italy Education 2000 Ph.D. thesis defence: “Structure and Function Relationships of Urease and Cytochrome c-553 from Bacillus pasteurii“York Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom 1996 - 2000 Study for a doctoral degree in Chemistry (c/o EMBL Hamburg) 1991 Master thesis, in Agricultural Science: “Allevamento in vitro delle larve di Pseudogonia rufifrons Wied. (Dipt. Tachinidae). Prove su diete subnaturali e meridiche“, 108/110. University of Bologna, Bologna Italy Main research areas Structural and functional characterization of proteins and enzymes from the phyopathogen Erwinia amylovora, the agent of fire blight, and of enzymes with a potential use in biotechnology. Bacterial iron metabolism, carbohydrate-active enzymes, metalloproteins. Since my appointment in Bolzano, I devoted myself to the development of the Bioorganic chemistry and Bio-Crystallography laboratory. In few years, my laboratory has characterized and solved the structure of several proteins that are deposited in the PDB. The most important achievement was the structural characterization of the complete biosynthetic pathway of desferrioxamine E, the siderophore of E. amylovora. This pathway includes a pyridoxal dependent lysine decarboxylase (DfoJ), a cadaverine monooxygenase (DfoA) and a desferrioxamine synthetase (DfoC). With the structure solution of the cysteine protease effector AvrRpt2 we shed light onto the induced mechanism of plant resistance to fire blight by Malus x robusta 5. We are the only laboratory using this approach to study the molecular basis of fire blight. During my PhD, my contribution was pivotal in the proposal of urease reaction mechanism by solving the structure of the enzyme from Sporosarcina pasteurii (previously Bacillus pasteurii) in the native form and in complex with several inhibitors.