Marco Mazzorana

Marco Mazzorana graduated in Organic Chemistry at the University of Padua under the direction of Prof. Giuseppe Zanotti. He then joined the group of Professor Lorenzo A. Pinna for his Ph.D. in Biochemistry and Biophysics. His thesis focused on the structural characterisation of protein kinase CK2 isoforms and of protein-inhibitor complexes.

After a short post-doc at the Venetian Institute of Molecular Medicine (VIMM, Padua) and three years at the Spanish National Cancer Research Centre (CNIO, Madrid), he joined Diamond Light Source as part of the I02 Beamline team in March 2011.

With Thomas Sorensen he studied gram negative bacteria membrane transport and cardiac calcium homeostasis integrating information from MX, SR-CD and SAXS with a multidisciplinary approach.

In the beamline he developed methods for room temperature and in-situ data collection and took part to the concept design of VMXi.

In the industrial liaison team, he provided expert scientific service to users conducting proprietary research in the MX beamlines. Besides his main role as local contact he designed and conducted bespoke experiments to address challenging scientific issues.

Back in the MX team after a research experience in the Biochemistry department of the University of Oxford, Marco has been in charge of the academic liaisons and the user scheduling for the five operational MX beamlines. He is actively involved in the streamlining of user experience, especially with the development, installation and commissioning of equipment and laboratories.

Structural biology of membrane proteins

Membrane proteins are fundamental to cell life and regulation. A large number of transporters, signalling and metabolic proteins are anchored to or are completely embedded in biological membranes. It has been estimated that a third of the human genome encodes for membrane proteins and for this reason they represent a growing field of research in structural biology. MsbA, a member of the large family of ATP-binding cassette transporters (ABC), hydrolyses ATP to promote the translocation of lipid A through the inner membrane of Gram negative bacteria. This is a crucial step to the formation of biofilms protecting bacteria such as Pseudomonas aeruginosa from the attack of the immune system are composed of lipid A. For this reason, MsbA and similar ABC-transporters represents a promising target of antibiotics research. I use biochemical and biophysical techniques to achieve better insight in the structure/function relationships of paMsbA, with particular emphasis in the crystallographic aspect and toward the design of new antibiotics.

Human calcium binding proteins

Calcium is widely exploited in eukaryotic cells, especially to trigger specific responses to signalling events. The release of calcium from intracellular stores triggers a number of cellular events, usually mediated by proteins such Calmodulin, which undergo major structural rearrangements upon Ca-binding. The cross-talk among various forms of signalling, including extracellular receptors, phosphorylation and other second messengers, are crucial for the correct tuning of the calcium response to stimuli. Spatial and temporal control of calcium signalling is therefore fundamental for muscle contraction, neurotransmission, cell growth and motility. A detailed structural description of these proteins and complexes would let us better understand the regulation of calcium signalling within eukaryotic cells. I am studying a group of calcium-binding proteins and their interactions with some of their regulators. In particular I am interested in the Sarco-Endoplasmic reticulum P-type Ca-ATPase (SERCA) and some of its functional partners. I make use of CD, SAXS and X-ray crystallography to understand how the crosstalk among these proteins finely regulates the contraction of the cardiac muscle.

Protein kinases and phosphatases

Post-translational modifications tagging proteins are widely used as molecular switches. In humans a large number of kinases and phosphatases control pathways by catalysing the reversible phosphorylation of nucleophilic protein side chains. Deregulation of the complex phosphorylation network of a cell often results in pathologies such as metabolic and proliferative diseases. For this reason, protein kinases are considered a hot topic both from academia and from pharmaceutical companies. Currently I am helping to develop techniques for the biochemical characterisation of some members of this class of enzymes. I am also continuing to work with older collaborations, on the structural description of kinase-inhibitor complexes as well as on protein phosphatases and their physiological modulators

Crystal handling tools

Together with the staff of the MX beamline I02, I am also working on novel crystal handling tools for the improvement of room temperature and humidity-controlled x-ray diffraction experiments.

Prof. Annamaria Brunati, Dr. Elena Tibaldi, Dr. Mario Pagano (University of Padua)

Prof. Cecilia Pozzi (University of Siena)

Dr. Danilo Belviso (CNR-IC, Bari)

Dr. Dritan Siliqi (CNR-IC, Bari)