Ban, Nenad - Eidgenössische Technische Hochschule Zürich - Department of Chemistry and Applied Biosciences

个人简介

Nenad Ban has been full Professor of structural molecular biology at ETH Zurich. He was born in Zagreb, Croatia and educated at the University of Zagreb where he obtained a BS degree in Molecular Biology. His main research interest at that time was the evolution of the components of the protein synthesis machinery. By the end of his studies, he received an award of the University of Zagreb for academic achievements. Dr. Ban's research interests during his Ph.D. study (1990-1994), at the University of California at Riverside, focused on structural immunology and virology. His continuing interest in the process of protein synthesis led him to the Department of Molecular Biophysics and Biochemistry at Yale University where he joined the group of Dr. Thomas Steitz as a Damon Runyon - Walter Winchell fund fellow and initiated the structural work on the large ribosomal subunit in the fall of 1995. The structure was completed by spring 2000, and during the last year of Dr. Ban-s stay at Yale University he was appointed in an independent position and established a small research group upon receiving a Burroughs Wellcome Career Award. The structure of the large ribosomal subunit provided first glimpses into the architecture of all cellular ribonucleoprotein particles and revealed that its active site is formed out of RNA making the ribosome a ribozyme. In 2002 Dr. Ban was a co-recipient of the Newcomb-Cleveland prize, awarded by the American Association for Advancement of Science, for this discovery. Since many clinically available antibacterial drugs inhibit the ribosome, the structure of the large ribosomal subunit has important implications on the development of new and improvement of existing antibiotics and in efforts to overcome bacterial drug resistance. Soon after the discovery was published, in the fall of 2000, Dr. Ban moved as an Assistant Professor of structural molecular biology to the Swiss Federal Institute of Technology in Zurich (ETH) where he expanded his group while maintaining the focus of his research interest towards better understanding of the protein synthesis process. At ETH, Dr. Ban is involved in directing research and teaching undergraduate and graduate level classes. Dr. Ban is married to Dr. Eilika Weber-Ban and they have a son, Arvid, who was born at the end of 2000 in Zürich.

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X-ray crystallographic structure determination of large asymmetric macromolecular assemblies Abrahams, Jan Pieter and Ban, Nenad (2003) The chemistry of protein synthesis and voyage through the ribosomal tunnel Jenni, Simon and Ban, Nenad (2003) High-resolution structures of ribosomal subunits and their complexes with substrates and antibiotics have revealed fundamental principles of template-directed protein synthesis. Mechanistic questions regarding ribosome function and catalysis can now be addressed with... Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB Gutmann, Sascha, Haebel, Peter W., Metzinger, Laurent, Sutter, Markus, Felden, Brice and Ban, Nenad (2003) Accurate translation of genetic information into protein sequence depends on complete messenger RNA molecules. Truncated mRNAs cause synthesis of defective proteins, and arrest ribosomes at the end of their incomplete message. In bacteria, a hybrid RNA molecule that combines the... Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module Berger, Philipp, Schaffitzel, Christiane, Berger, Imre, Ban, Nenad and Suter, Ueli (2003) Mutations in the myotubularin (MTM)-related protein 2 (MTMR2) gene are responsible for the severe autosomal recessive neuropathy Charcot-Marie-Tooth disease type 4B1. MTMR2 belongs to the MTM family of dual-specific phosphatases that use phosphatidylinositol (PI) 3,5-bisphosphate... Structural basis of protein synthesis Schaffitzel, Christiane and Ban, Nenad (2004) Dial tm for rescue Haebel, Peter W., Gutmann, Sascha and Ban, Nenad (2004) Ribosomes translate genetic information encoded by mRNAs into protein chains with high fidelity. Truncated mRNAs lacking a stop codon will cause the synthesis of incomplete peptide chains and stall translating ribosomes. In bacteria, a ribonucleoprotein complex composed of tmRNA, a... Structure and functional analysis of the fungal galectin CGL2 Walser, Piers J., Haebel, Peter W., Künzler, Markus, Sargent, David, Kües, Ursula, Aebi, Markus and Ban, Nenad (2004) Recognition of and discrimination between potential glyco-substrates is central to the function of galectins. Here we dissect the fundamental parameters responsible for such selectivity by the fungal representative, CGL2. The 2.1 Angstrom crystal structure of CGL2 and five... Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins Ferbitz, Lars, Maier, Timm, Patzelt, Holger, Bukau, Bernd, Deuerling, Elke and Ban, Nenad (2004) During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state(1,2). Here we present a 2.7 Angstrom crystal structure of Escherichia coli trigger factor, the... The structural basis of macrolide-ribosome binding assessed using mutagenesis of 23 S rRNA positions 2058 and 2059 Pfister, Peter, Jenni, Simon, Poehlsgaard, Jacob, Thomas, Ashley, Douthwaite, Stephen, Ban, Nenad and Böttger, Erik C. (2004) Macrolides are a diverse group of antibiotics that inhibit bacterial growth by binding within the peptide tunnel of the 50 S ribosomal subunit. There is good agreement about the architecture of the macrolide site from different crystallography studies of bacterial and archaeal 50 S... Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors Leibundgut, Marc, Frick, Christian, Thanbichler, Martin, Böck, August and Ban, Nenad (2005) In all three kingdoms of life, SelB is a specialized translation elongation factor responsible for the cotranslational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop. Here, we present the X- ray... Target-directed proteolysis at the ribosome Henrichs, Tanja, Mikhaleva, Natasha, Conz, Charlotte, Deuerling, Elke, Boyd, Dana, Zelazny, Adrian, Bibi, Eitan, Ban, Nenad and Ehrmann, Michael (2005) Target directed proteolysis allows specific processing of proteins in vivo. This method uses tobacco etch virus (TEV) Nla protease that recognizes a seven-residue consensus sequence. Because of its specificity, proteins engineered to contain a cleavage site are proteolysed, whereas... A cradle for new proteins Maier, Timm, Ferbitz, Lars, Deuerling, Elke and Ban, Nenad (2005) Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During ongoing synthesis, nascent protein chains are particularly sensitive to aggregation and degradation because they emerge from the ribosome in an unfolded state. In bacteria, the first... Cytosolic proteins at birth Ferbitz, Lars, Maier, Timm, Patzelt, Holger, Bukau, Bernd, Ban, Nenad and Deuerling, Elke (2005) Structure of the E-coli protein-conducting channel bound to a translating ribosome Mitra, Kakoli, Schaffitzel, Christiane, Shaikh, Tanvir, Tama, Florence, Jenni, Simon, Brooks, Charles L., Ban, Nenad and Frank, Joachim (2005) Secreted and membrane proteins are translocated across or into cell membranes through a protein-conducting channel (PCC). Here we present a cryo-electron microscopy reconstruction of the Escherichia coli PCC, SecYEG, complexed with the ribosome and a nascent chain containing a... Architecture of Mammalian Fatty Acid Synthase at 4.5 Å Resolution Maier, Timm, Jenni, Simon and Ban, Nenad (2006) The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom–resolution x-ray... Selenium metabolism in prokaryotes Böck, August, Rother, Michael, Leibundgut, Marc and Ban, Nenad (2006) The biosynthesis and specific incorporation of selenocysteine into protein requires the function of a UGA codon determining the position of selenocysteine insertion and a secondary/tertiary structure within the mRNA, designated the SECIS element, following the UGA at its... Architecture of a fungal fatty acid synthase at 5 angstrom resolution Jenni, Simon, Leibundgut, Marc, Maier, Timm and Ban, Nenad (2006) All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha(6)beta(6) complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual... Architecture of Mammalian Fatty Acid Synthase at 4.5 Å Resolution Maier, Timm, Jenni, Simon and Ban, Nenad (2006) The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic... Architecture of a Fungal Fatty Acid Synthase at 5 Å Resolution Jenni, Simon, Leibundgut, Marc, Maier, Timm and Ban, Nenad (2006) All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha(6)beta(6) complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the... Structure of the Eukaryotic Thiamine Pyrophosphate Riboswitch with Its Regulatory Ligand Thore, Stéphane, Leibundgut, Marc and Ban, Nenad (2006) Riboswitches are untranslated regions of messenger RNA, which adopt alternate structures, depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the...