We have now opened up the application for projects to the ISB Postdoctoral program. If you are a Umeå University PI with interest in structural biology research, please see here for information on how to participate in the program.
Martínez-Carranza M, Blasco P, Gustafsson R, Dong M, Berntsson RP, Widmalm G, Stenmark P. Synaptotagmin Binding to Botulinum Neurotoxins. Biochemistry in press. doi: 10.1021/acs.biochem.9b00554
In an article in the latest issue of “Kemisk Tidskrift” Jonas Baranduns “tiny” ribosome structure is shown together with an update on ISB in Umeå!!
A new study from the Barandun research group in collaboration with researchers at The Rockefeller University and The Connecticut Agricultural Experiment station uncovers the cryo-EM structure of the smallest known eukaryotic cytoplasmic ribosome. The structure visualizes the effect of extreme genome compaction on the translation machinery in microsporidia, uncovers a species-specific ribosomal protein and suggests a novel mode of ribosome inhibition in eukaryotes.
Barandun, J., Hunziker, M., Vossbrinck, C. R. & Klinge, S. Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome. Nat. Microbiol. (2019). in press. doi:10.1038/s41564-019-0514-6
Involved research groups:
Barandun research group
The Laboratory for Molecular Infection Medicine Sweden (MIMS) and SciLifeLab National Fellow
Department of Molecular Biology
Laboratory of Protein and Nucleic Acid Chemistry, Klinge Lab
The Rockefeller University, New York, USA
Department of Environmental Sciences
The Connecticut Agricultural Experiment Station
New Haven, CT, USA
In a computational study by ISB member Kwangho Nam (Umeå and UT Arlington) and Martin Karplus (Harvard University) a detailed model has been developed for the coupling between rotary motion and ATP hydrolysis in F1-ATPase. The model predicts that F1-ATPase functions at near its maximum possible efficiency. The finding is published in PNAS. https://www.pnas.org/content/116/32/15924.long
In an ISB effort the research groups lead by Anna Linusson, Elisabeth Sauer-Eriksson and Magnus Wolf-Watz has discovered a key event in activation of the essential enzyme adenylate kinase. It was discovered that the large-scale and activating conformational change triggered by ATP binding is nucleated by a strong cation-PI interaction formed between the cationic sidechain of an arginine with the aromatic adenosine base of ATP. The discovery may pave way for future enzyme design efforts where recognition of aromatic systems is required. The finding was made possible through an integrative effort using DFT calculations, NMR spectroscopy and x-ray crystallography. The team consisted of Per Rogne, David Andersson, Christin Grundström, Elisabeth Sauer-Eriksson, Anna Linusson and Magnus Wolf-Watz. The finding is published in Biochemistry https://pubs.acs.org/doi/10.1021/acs.biochem.9b00538.
A fully funded PhD position is available in Karina Persson’s group. The overall aim of the project is to obtain structural and functional data of bacterial fimbrial proteins and associated proteins involved in maturation of fimbria For more information and how to apply:
The closing date for applications is the 5th of Aug. 2019.
We are happy to announce that the Kempe foundation is funding an ISB postdoc program with two fellowships 2019 and three fellowships 2020. Running costs are included for the positions. The program will fund new constellations that tackle interdisciplinary structural biology projects. For more information please go to the page ISB Postdoctoral program.
Please, follow this link to apply or for more information.
Krypotou, E., Scortti, M., Grundström, C., Oelker, M., Luisi, B.F., Sauer-Eriksson, A.E. & Vázquez-Boland, J. Control of bacterial virulence through the peptide signature of the habitat. (2019) Cell Reports, 26, 1815-1827.
We identify a major control mechanism of Listeria virulence based on antagonistic regulation by environmental peptides.Activity levels of the virulence regulator PrfA depend on the net balance between the rates of synthesis of the PrfA-activating cofactor GSH from exogenous peptide-derived cysteine and of direct, promiscuous PrfA inhibition by non-cysteine-containing peptides