Giuseppe Zanotti graduated in chemistry in Padua in 1974 and he is now Full Professor at the Department of Biomedical Sciences of the same University. Since the beginning of its scientific career he has worked at the determination of the structure of molecules and macromolecules through x-ray diffraction. After a Dr degree dissertation on bovine pancreatic Ribonuclease, he has been always active in the field of structural biology. In 1979-80 he has spent one year at the Laboratory of Molecular Biophysics in Oxford, working with Louise Johnson on the structure of glycogen phosphorylase b. Back to Padua, he has been interested in proteins that bind and transport small hydrophobic molecules, in the structural determination of protein kinase CK2/inhibitor complexes and, more recently, in that of proteins from pathogenic bacteria, in particular H. pylori.
Giuseppe Zanotti has also been interested in theoretical aspects of the phase problem in crystallography and on the analysis and conformational aspects of the structure of globular proteins.
He has published 173 papers on international journals, 14 book chapters and some didactic books. He has deposited more than 100 protein structures at the PDB (http://www.rcsb.org).

The research project presented by the candidate perfectly fits both with the main scientific interest of my research lab (H. pylori) and with my crystallographic expertise.

Honors
1. 2007, Mario Mammi Prize from the Italian Crystallographic Society (AIC).
2. 2008-present, Chairman of the Doctorate School in Biochemistry and Biotechnology
3. 2002-present, Chairman of the Review Committee of Protein Crystallography of Elettra Sinchrotron (Trieste), Member of the BiostructX review panel, member of the ESRF synchtrono Facility evaluation panel.

Structural proteomics of Helicobacter pylori. H. pylori chronically infects the gastric mucosa of the majority of the human population, and it is implicated in the development of severe gastroduodenal diseases, including active chronic gastritis, peptic ulcers, gastric adenocarcinoma and mucosa-associated lymphoma. This bacterium is interesting not only because it is a human pathogen not totally understood, but also for other reasons: it lives only in a very special niche, the human stomach, and during evolution he has adapted to this peculiar and hard environment. Its genome (the genomes of three different strains have been sequenced) codes for about 1500 hypothetical genes, but bioinformatics analysis allows to assign a tentative function to about only 2/3 of these genes, suggesting a specialized and peculiar evolution of HP with respect to other well known gram-negative bacteria, like E. coli. We plan to use HP as a paradigm of a special, relatively simple prokaryote and to try to define all its components in terms of molecular structures, functions and inter-relationships. In the past, we have determined the crystal structure of the neutrophil activating protein (HP-NAP), a 200 kDa oligomer capable of promoting neutrophil adhesion to endothelial cells and of inducing neutrophils to produce reactive oxygen radicals, and of alkyl hydroperoxide-reductase. We now concentrate on factors involved in pathogenicity and in the proteins essential for the bacterium colonization and persistence.
The work of the Structural Biology unit of the group focuses on the structural characterization of proteins involved in both the two major objectives of the project: 1) Persistence/antibiotic resistance and 2) Latency/virulence/interaction with the host.
Structural characterization of Calcium-binding proteins. We have crystallized and determined the crystal structure of the Calcium pump of the sarcoplasmic reticulum (SERCA) from bovine muscle and we plan to determine the structure of different SERCA isoforms and of mutants responsible of different pathologies. We are also trying to crystallize the calcium mitochondrial uniporter (MCU) and its partner MICU1.

Selected publications
2.C. FOLLI, V. CALDERONE, S. OTTONELLO, A. BOLCHI, G. ZANOTTI, M. STOPPINI AND R. BERNI " Identification, retinoid binding and X-ray analysis of a novel human retinol-binding protein" Proc. Nat. Acad. Sci. (2001) 98, 3710-3715
4.E. PAPINUTTO, W. G. DUNDON, N. PITULIS, R. BATTISTUTTA, C. MONTECUCCO, AND G. ZANOTTI "Structure of two iron-binding proteins from Bacillus anthracis " J. Biol. Chem., (2002) 277, 15093-15098
5.V. CALDERONE, C. FOLLI, A. MARCHESANI, R. BERNI AND G. ZANOTTI "Identification and structural analysis of a zebrafish apo and holo cellular retinol-binding protein", J. Mol. Biol. (2002) 321, 527-535
6.G. ZANOTTI, E. PAPINUTTO, W.G. DUNDON, R. BATTISTUTTA, M. SEVESO, G. DEL GIUDICE, R. RAPPUOLI,, AND C. MONTECUCCO Structure of the neutrophil activating protein from Helicobacter pylori J. Mol. Biol., (2002) 323, 125-130
7. C. FOLLI, V. CALDERONE, I. RAMAZZINA AND G. ZANOTTI "Ligand Binding and Structural Analysis of a Human Putative Cellular Retinol-binding Protein" J. Biol. Chem. (2002) 277, 41970-41977
8.E. DE MOLINER, S. MORO, S. SARNO, G. ZAGOTTO, G. ZANOTTI, L. A. PINNA & R. BATTISTUTTA Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight. J. Biol. Chem. (2003) 278, 1831-1836
9.CALDERONE, R. BERNI AND G. ZANOTTI "High-resolution Structures of Retinol-Binding Protein in Complex with Retinol: pH-induced Protein Structural Changes in the Crystal State" J. Mol. Biol. (2003) 329, 841-850
10. V. CALDERONE, M. TRABUCCO, A. VUJICIC, R. BATTISTUTTA, G. M. GIACOMETTI, F. ANDREUCCI, R. BARBATO, G. ZANOTTI "Crystal structure of the PsbQ polypeptide of photosystem II from higher plants" EMBO reports (2003) 4, 894-899
11.L. CENDRON, A. SEYDEL, A. ANGELINI, R. BATTISTUTTA, AND G. ZANOTTI "Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system" J. Mol. Biol. (2004) 340, 881-889
12.M. LUNELLI, M.L. DI PAOLO, M. BIADENE, V. CALDERONE, R. BATTISTUTTA, M. SCARPA, A. RIGO AND G. ZANOTTI “Crystal structure of amine oxidase from bovine serum” J. Mol. Biol. (2005) 346, 991-1004
13. N. PASQUATO, R. BERNI, C. FOLLI, S. FOLLONI, M. CIANCI, S. PANTANO, J.R. HELLIWELL AND G. ZANOTTI “Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens” J. Mol. Biol. (2006) 356, 684-694
14. G. ZANOTTI, L. CENDRON, I. RAMAZZINA, C. FOLLI, R. PERCUDANI, AND R. BERNI “Structure of zebrafish HIUase: Insights into evolution of an enzyme to a hormone transporter ” J. Mol. Biol. (2006) 363, 1-9
15. N. PASQUATO, R. BERNI, C. FOLLI, B. ALFIERI, L. CENDRON AND G. ZANOTTI “Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin” J. Mol. Biol. (2007) 366, 711-719
16. L. CENDRON, R. BERNI, C. FOLLI, I. RAMAZZINA, R. PERCUDANI AND G. ZANOTTI “The structure of 2-OXO-4-HYDROXY-4-CARBOXY-5- UREIDOIMIDAZOLINE DECARBOXYLASE provides insight into the mechanism of uric acid degradation” J. Biol. Chem., (2007), 282, 18182-18189
17.I. RAMAZZINA, L. CENDRON, C. FOLLI, R. BERNI, D. MONTEVERDI, G. ZANOTTI, AND R. PERCUDANI "Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases" J. Biol. Chem. (2008) 283, 23295-23304
18. L. CENDRON, M. COUTURIER, A. ANGELINI, N. BARISON, M. STEIN AND G. ZANOTTI “The Helicobacter pylori CagD (HP0545, Cag24) protein is required for CagA translocation but not for type IV secretion pilus assembly” J. Mol. Biol. (2009) 386, 204-217
19. L. CENDRON, A. TROVATO, F. SENO, C. FOLLI, B. ALFIERI, G. ZANOTTI AND R. BERNI “Amyloidogenic potential of transthyretin variants: insights from structural and computational analysis” J. Biol. Chem. (2009) 284, 25832-25841
20. I. RAMAZZINA, R. COSTA, L. CENDRON, R. BERNI, A. PERACCHI, G. ZANOTTI, AND R. PERCUDANI “An aminotransferase branch point connects purine catabolism to amino acid recycling” Nature Chem. Biol. (2010), 6, 801-806
21. G. ZANOTTI AND L. CENDRON “Structural and functional aspects of Helicobacter pylori acidic stress response” IUBMB Life (2010), 62, 715-723
22. L. CENDRON, I. RAMAZZINA, R. PERCUDANI, C. RASORE, G. ZANOTTI, R. BERNI “Probing the evolution of hydroxyisourate hydrolase into transthyretin through active site redesign” J. Mol. Biol., (2011) 409, 504-512
23. L. CENDRON, P. BERTO, S. D’ADAMO, F. VALLESE, C. GOVONI, M.C. POSEWITZ, G.M GIACOMETTI, P. COSTANTINI, G. ZANOTTI “Crystal structure of YhdF scaffold protein provides insights into [FeFe]-hydrogenase maturation” J. Biol. Chem. (2011), 286, 43944-43950

No projects are available to students for the current accademic year.