TY - THES A1 - Müller, Jürgen J. T1 - A real-time in-memory discovery service Y1 - 2012 CY - Potsdam ER - TY - JOUR A1 - Müller, Jürgen J. A1 - Barbirz, Stefanie A1 - Heinle, Karolin A1 - Freiberg, Alexander A1 - Seckler, Robert A1 - Heinemann, Udo T1 - An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri phage Sf6 N2 - Sf6 belongs to the Podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded DNA. They attach to their hosts specifically via their tailspike proteins. The 1.25 Å crystal structure of Shigella phage Sf6 tailspike protein (Sf6 TSP) reveals a conserved architecture with a central, right-handed ; helix. In the trimer of Sf6 TSP, the parallel ; helices form a left-handed, coiled;; coil with a pitch of 340 Å. The C-terminal domain consists of a ; sandwich reminiscent of viral capsid proteins. Further crystallographic and biochemical analyses show a Shigella cell wall O-antigen fragment to bind to an endorhamnosidase active site located between two ;-helix subunits each anchoring one catalytic carboxylate. The functionally and structurally related bacteriophage, P22 TSP, lacks sequence identity with Sf6 TSP and has its active sites on single subunits. Sf6 TSP may serve as an example for the evolution of different host specificities on a similar general architecture. Y1 - 2008 UR - http://www.cell.com/structure/abstract/S0969-2126%2808%2900106-8 U6 - https://doi.org/10.1016/j.str.2008.01.019 ER - TY - JOUR A1 - Klein, Julia A1 - Darvin, Maxim E. A1 - Meinke, Martina C. A1 - Schweigert, Florian J. A1 - Müller, Kerstin E. A1 - Lademann, Jürgen T1 - Analyses of the correlation between dermal and blood carotenoids in female cattle by optical methods JF - Journal of biomedical optics N2 - Herd health programs for the maintenance of welfare and productivity in cattle need efficient tools for monitoring the health of individual animals. Recent reports demonstrate that the oxidative status is related to various stress conditions in dairy cows. Biomarkers, among other carotenoids, could serve as indicators of stress originating from the environment (e.g., heat stress or sun radiation) or from the animal itself (e.g., disease). To date, only invasive in vitro tests are available to assess the oxidative status in cattle. The present study compares the results of optical noninvasive in vivo measurements of dermal carotenoids in cattle udder skin using an LED-based miniaturized spectroscopic system (MSS) with those obtained by photometric analysis of beta carotene in whole blood samples using a portable device. Correlations between the concentrations of dermal and blood carotenoids were calculated under consideration of the nutritional status of the animals. Significant correlation (R = 0.86) was found for cattle with a moderate to obese body condition. Thus, the blood and skin concentrations of the marker substance beta carotene are comparable under stable stress conditions of the cattle. This demonstrates that the MSS is suitable for noninvasive assessment of dermal carotenoid concentrations in cattle. KW - Raman spectroscopy KW - reflection spectroscopy KW - skin KW - antioxidants KW - free radicals Y1 - 2013 U6 - https://doi.org/10.1117/1.JBO.18.6.061219 SN - 1083-3668 VL - 18 IS - 6 PB - SPIE CY - Bellingham ER - TY - JOUR A1 - Seul, Anait A1 - Müller, Jürgen J. A1 - Andres, Dorothee A1 - Stettner, Eva A1 - Heinemann, Udo A1 - Seckler, Robert T1 - Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker JF - Acta crystallographica : Section D, Biological crystallography N2 - Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection. Y1 - 2014 U6 - https://doi.org/10.1107/S1399004714002685 SN - 1399-0047 VL - 70 SP - 1336 EP - 1345 PB - Wiley-Blackwell CY - Hoboken ER - TY - JOUR A1 - Damaschun, Gregor A1 - Damaschun, Hilde A1 - Gast, Klaus A1 - Misselwitz, Rolf A1 - Müller, Jürgen J. A1 - Pfeil, Wolfgang A1 - Zirwer, Dietrich T1 - Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast Y1 - 1993 ER - TY - JOUR A1 - Barbirz, Stefanie A1 - Müller, Jürgen J. A1 - Uetrecht, Charlotte A1 - Clark, Alvin J. A1 - Heinemann, Udo A1 - Seckler, Robert T1 - Crystal structure of Escherichia coli phage HK620 tailspike : podoviral tailspike endoglycosidase modules are evolutionarily related N2 - Bacteriophage HK620 infects Escherichia coli H and is closely related to Shigella phage Sf6 and Salmonella phage P22. All three Podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. The three proteins exhibit high sequence identity in the 110 residues of their N-terminal particle- binding domains, but no apparent sequence similarity in their major, receptor-binding parts. We have biochemically characterized the receptor-binding part of HK620 tailspike and determined its crystal structure to 1.38 Å resolution. Its major domain is a right-handed parallel ;-helix, as in Sf6 and P22 tailspikes. HK620 tailspike has endo-N- acetylglucosaminidase activity and produces hexasaccharides of an O18A1-type O-antigen. As indicated by the structure of a hexasaccharide complex determined at 1.6 Å resolution, the endoglycosidase-active sites are located intramolecularly, as in P22, and not between subunits, as in Sf6 tailspike. In contrast, the extreme C-terminal domain of HK620 tailspike forms a ;-sandwich, as in Sf6 and unlike P22 tailspike. Despite the different folds, structure-based sequence alignments of the C-termini reveal motifs conserved between the three proteins. We propose that the tailspike genes of P22, Sf6 and HK620 have a common precursor and are not mosaics of unrelated gene fragments. Y1 - 2008 UR - http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2008.06311.x/pdf SN - 0950-382X ER - TY - CHAP A1 - Kurbel, Karl A1 - Nowak, Dawid A1 - Azodi, Amir A1 - Jaeger, David A1 - Meinel, Christoph A1 - Cheng, Feng A1 - Sapegin, Andrey A1 - Gawron, Marian A1 - Morelli, Frank A1 - Stahl, Lukas A1 - Kerl, Stefan A1 - Janz, Mariska A1 - Hadaya, Abdulmasih A1 - Ivanov, Ivaylo A1 - Wiese, Lena A1 - Neves, Mariana A1 - Schapranow, Matthieu-Patrick A1 - Fähnrich, Cindy A1 - Feinbube, Frank A1 - Eberhardt, Felix A1 - Hagen, Wieland A1 - Plauth, Max A1 - Herscheid, Lena A1 - Polze, Andreas A1 - Barkowsky, Matthias A1 - Dinger, Henriette A1 - Faber, Lukas A1 - Montenegro, Felix A1 - Czachórski, Tadeusz A1 - Nycz, Monika A1 - Nycz, Tomasz A1 - Baader, Galina A1 - Besner, Veronika A1 - Hecht, Sonja A1 - Schermann, Michael A1 - Krcmar, Helmut A1 - Wiradarma, Timur Pratama A1 - Hentschel, Christian A1 - Sack, Harald A1 - Abramowicz, Witold A1 - Sokolowska, Wioletta A1 - Hossa, Tymoteusz A1 - Opalka, Jakub A1 - Fabisz, Karol A1 - Kubaczyk, Mateusz A1 - Cmil, Milena A1 - Meng, Tianhui A1 - Dadashnia, Sharam A1 - Niesen, Tim A1 - Fettke, Peter A1 - Loos, Peter A1 - Perscheid, Cindy A1 - Schwarz, Christian A1 - Schmidt, Christopher A1 - Scholz, Matthias A1 - Bock, Nikolai A1 - Piller, Gunther A1 - Böhm, Klaus A1 - Norkus, Oliver A1 - Clark, Brian A1 - Friedrich, Björn A1 - Izadpanah, Babak A1 - Merkel, Florian A1 - Schweer, Ilias A1 - Zimak, Alexander A1 - Sauer, Jürgen A1 - Fabian, Benjamin A1 - Tilch, Georg A1 - Müller, David A1 - Plöger, Sabrina A1 - Friedrich, Christoph M. A1 - Engels, Christoph A1 - Amirkhanyan, Aragats A1 - van der Walt, Estée A1 - Eloff, J. H. P. A1 - Scheuermann, Bernd A1 - Weinknecht, Elisa ED - Meinel, Christoph ED - Polze, Andreas ED - Oswald, Gerhard ED - Strotmann, Rolf ED - Seibold, Ulrich ED - Schulzki, Bernhard T1 - HPI Future SOC Lab BT - Proceedings 2015 N2 - Das Future SOC Lab am HPI ist eine Kooperation des Hasso-Plattner-Instituts mit verschiedenen Industriepartnern. Seine Aufgabe ist die Ermöglichung und Förderung des Austausches zwischen Forschungsgemeinschaft und Industrie. Am Lab wird interessierten Wissenschaftlern eine Infrastruktur von neuester Hard- und Software kostenfrei für Forschungszwecke zur Verfügung gestellt. Dazu zählen teilweise noch nicht am Markt verfügbare Technologien, die im normalen Hochschulbereich in der Regel nicht zu finanzieren wären, bspw. Server mit bis zu 64 Cores und 2 TB Hauptspeicher. Diese Angebote richten sich insbesondere an Wissenschaftler in den Gebieten Informatik und Wirtschaftsinformatik. Einige der Schwerpunkte sind Cloud Computing, Parallelisierung und In-Memory Technologien. In diesem Technischen Bericht werden die Ergebnisse der Forschungsprojekte des Jahres 2015 vorgestellt. Ausgewählte Projekte stellten ihre Ergebnisse am 15. April 2015 und 4. November 2015 im Rahmen der Future SOC Lab Tag Veranstaltungen vor. KW - Future SOC Lab KW - Forschungsprojekte KW - Multicore Architekturen KW - In-Memory Technologie KW - Cloud Computing KW - maschinelles Lernen KW - künstliche Intelligenz Y1 - 2017 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-102516 ER - TY - JOUR A1 - Bröker, Nina Kristin A1 - Gohlke, Ulrich A1 - Müller, Jürgen J. A1 - Uetrecht, Charlotte A1 - Heinemann, Udo A1 - Seckler, Robert A1 - Barbirz, Stefanie T1 - Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity JF - Glycobiology N2 - Bacteriophage HK620 recognizes and cleaves the O-antigen polysaccharide of Escherichia coli serogroup O18A1 with its tailspike protein (TSP). HK620TSP binds hexasaccharide fragments with low affinity, but single amino acid exchanges generated a set of high-affinity mutants with submicromolar dissociation constants. Isothermal titration calorimetry showed that only small amounts of heat were released upon complex formation via a large number of direct and solvent-mediated hydrogen bonds between carbohydrate and protein. At room temperature, association was both enthalpy- and entropy-driven emphasizing major solvent rearrangements upon complex formation. Crystal structure analysis showed identical protein and sugar conformers in the TSP complexes regardless of their hexasaccharide affinity. Only in one case, a TSP mutant bound a different hexasaccharide conformer. The extended sugar binding site could be dissected in two regions: first, a hydrophobic pocket at the reducing end with minor affinity contributions. Access to this site could be blocked by a single aspartate to asparagine exchange without major loss in hexasaccharide affinity. Second, a region where the specific exchange of glutamate for glutamine created a site for an additional water molecule. Side-chain rearrangements upon sugar binding led to desolvation and additional hydrogen bonding which define this region of the binding site as the high-affinity scaffold. KW - bacterial O-antigen KW - carbohydrate interaction KW - site-directed mutagenesis KW - structural thermodynamics KW - tailspike protein Y1 - 2013 U6 - https://doi.org/10.1093/glycob/cws126 SN - 0959-6658 VL - 23 IS - 1 SP - 59 EP - 68 PB - Oxford Univ. Press CY - Cary ER -