Locher, Kaspar - Eidgenössische Technische Hochschule Zürich - Department of Chemistry and Applied Biosciences

个人简介

Kaspar Locher is Associate Professor of Molecular Membrane Biology at the Institute of Molecular Biology and Biophysics at ETH Zurich.Kaspar Locher pursued studies in biochemistry at the Swiss Federal Institute of Technology (ETH) Zurich from 1989-1994. He moved on to the laboratory of Prof. J. Rosenbusch at the Biozentrum, University of Basel, where he obtained his PhD in 1998. From 1999 to 2003, he was a post-doctoral researcher in the laboratory of Prof. Douglas Rees at the California Institute of Technology. In 2003, he joined ETH Zurich as Assistant Professor and was promoted to Associate Professor in 2008.His research focus is the structure and function of membrane transport proteins. These ubiquitous proteins facilitate the uptake of nutrients and the extrusion of toxic substances across cell membranes. To understand the transport mechanism, the three-dimensional structures of these proteins are determined at high resolution using X-ray crystallography.

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ABC transporter architecture and mechanism Locher, Kaspar P. and Borths, Elizabeth (2004) ABC transporters are ubiquitous membrane proteins that facilitate unidirectional substrate translocation across the lipid bilayer. Over the past five years, new crystal structures have advanced our understanding of how ABC transporters couple adenosine triphosphate (ATP) hydrolysis... In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B-12 uptake Structure of a bacterial multidrug ABC transporter Dawson, Roger J.P. and Locher, Kaspar P. (2006) Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined... Structural Studies of ABC Transporters Rees, Douglas C., Lee, Allen T., Locher, Kaspar P. and Pinkett, Heather W. (2006) ABC transporters form a ubiquitous family of importer and exporter proteins that translocate their ligands across the membrane against a concentration gradient. Members of this family invariably consist of two well conserved cytoplasmic ABC (ATP Binding Cassette) domains that power... Structure of an ABC transporter in complex with its binding protein Hollenstein, Kaspar, Frei, Dominik C. and Locher, Kaspar P. (2007) ATP-binding cassette (ABC) transporter proteins carry diverse substrates across cell membranes(1). Whereas clinically relevant ABC exporters are implicated in various diseases or cause multidrug resistance of cancer cells(2,3), bacterial ABC importers are essential for... Uptake or extrusion Dawson, Roger J.P., Hollenstein, Kaspar and Locher, Kaspar P. (2007) ATP-binding cassette (ABC) transporters are integral membrane proteins that move diverse substrates across cellular membranes. ABC importers catalyse the uptake of essential nutrients from the environment, whereas ABC exporters facilitate the extrusion of various... Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Hvorup, Rikki N., Goetz, Birke A., Niederer, Martina, Hollenstein, Kaspar, Perozo, Eduardo and Locher, Kaspar P. (2007) BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B-12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes... Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP Dawson, Roger J.P. and Locher, Kaspar P. (2007) Staphylococcus aureus Sav1866 is a bacterial homolog of the human ABC transporter Mdr1 that causes multidrug resistance in cancer cells. We report the crystal structure of Sav1866 in complex with adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP) at 3.4 angstrom resolution and... Structure and mechanism of ABC transporter proteins Hollenstein, Kaspar, Dawson, Roger J.P. and Locher, Kaspar P. (2007) ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins that couple the transport of diverse substrates across cellular membranes to the hydrolysis of ATP. The crystal structures of four ABC transporters have recently been determined. They reveal similar... Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter Gerber, Sabina, Comellas-Bigler, Mireia, Goetz, Birke A. and Locher, Kaspar P. (2008) Transport across cellular membranes is an essential process that is catalyzed by diverse membrane transport proteins. The turnover rates of certain transporters are inhibited by their substrates in a process termed trans- inhibition, whose structural basis is poorly understood. We... Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking Goetz, Birke A., Perozo, Eduardo and Locher, Kaspar P. (2009) BtuCD is a type II ABC importer that catalyzes the translocation of vitamin B12 from the periplasm into the cytoplasm of Escherichia coli. Crystal structures of BtuCD and the related HiF (or Hi1470/71) protein from Haemophilus influenzae have revealed distinct... Structure and mechanism of ATP-binding cassette transporters Locher, Kaspar P. (2009) ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These... Distorted octahedral coordination of tungstate in a subfamily of specific binding proteins Hollenstein, Kaspar, Comellas-Bigler, Mireia, Bevers, Loes E., Feiters, Martin C., Meyer-Klaucke, Wolfram, Hagedoorn, Peter-Leon and Locher, Kaspar P. (2009) Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO4 2−) and tungstate (WO4 2−). These substrates are captured by an external, high-affinity binding protein, and delivered to ATP binding cassette transporters,... A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation Lewinson, Oded, Lee, Allen T., Locher, Kaspar P. and Rees, Douglas C. (2010) ATP-binding cassette (ABC) transporters are integral membrane proteins that translocate a diverse array of substrates across cell membranes. We present here the dynamics of complex formation of three structurally characterized ABC transporters-the BtuCD vitamin B-12 importer and... In Vitro Folding and Assembly of the Escherichia coli ATP-binding Cassette Transporter, BtuCD Di Bartolo, Natalie D., Hvorup, Rikki N., Locher, Kaspar P. and Booth, Paula J. (2011) Studies on membrane protein folding have focused on monomeric alpha-helical proteins and a major challenge is to extend this work to larger oligomeric membrane proteins. Here, we study the Escherichia coli (E. coli) ATP-binding cassette (ABC) transporter that imports vitamin B-12... X-ray structure of a bacterial oligosaccharyltransferase Lizak, Christian, Gerber, Sabina, Numao, Shin, Aebi, Markus and Locher, Kaspar P. (2011) Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organism development or... Transmembrane Gate Movements in the Type II ATP-binding Cassette (ABC) Importer BtuCD-F during Nucleotide Cycle Joseph, Benesh, Jeschke, Gunnar, Goetz, Birke A., Locher, Kaspar P. and Bordignon, Enrica (2011) ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that translocate substrates across cell membranes. The alternating access of their transmembrane domains to opposite sides of the membrane powered by the closure and reopening of the nucleotide... X-ray structure of the Yersinia pestis heme transporter HmuUV Woo, Jae-Sung, Zeltina, Antra, Goetz, Birke A. and Locher, Kaspar P. (2012) HmuUV is a bacterial ATP-binding cassette (ABC) transporter that catalyzes heme uptake into the cytoplasm of the Gram-negative pathogen Yersinia pestis. We report the crystal structure of HmuUV at 3.0 angstrom resolution in a nucleotide-free state, which features a heme... Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF Korkhov, Vladimir M., Mireku, Samantha A., Hvorup, Rikki N. and Locher, Kaspar P. (2012) BtuCD is an ABC transporter catalyzing the uptake of vitamin B12 across the Escherichia coli inner membrane. A previously reported X-ray structure of BtuCD in complex with the periplasmic vitamin B12-binding protein BtuF revealed asymmetry of the transmembrane BtuC subunits. The... Asymmetric states of vitamin B-12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF Korkhov, Vladimir M., Mireku, Samantha A., Hvorup, Rikki N. and Locher, Kaspar P. (2012) BtuCD is an ABC transporter catalyzing the uptake of vitamin B-12 across the Escherichia coli inner membrane. A previously reported X-ray structure of BtuCD in complex with the periplasmic vitamin B-12-binding protein BtuF revealed asymmetry of the transmembrane BtuC subunits. The...