Jonas Barandun featured in “Kemisk Tidskrift” article

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!!

New article in Nature Microbiology: Evolutionary compaction and adaptation visualized by the structure of the dormant microsporidian ribosome

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

Klinge laboratory
Laboratory of Protein and Nucleic Acid Chemistry, Klinge Lab
The Rockefeller University, New York, USA

Vossbrinck laboratory
Department of Environmental Sciences 
The Connecticut Agricultural Experiment Station
New Haven, CT, USA

Image Attributions

  1. “Corn (Zea mays): Corn earworm (Helicoverpa zea)” by Plant pests and diseases is licensed under CC PDM 1.0 
  2. Vairimorpha necatrix spores, picture by Charles R. Vossbrinck

F1-ATPase function uncovered with computational structural biology

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.

Mechanism of enzyme activation discovered

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

PhD position in Karina Persson’s group

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.

Postdoctoral program

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.

New Article in Cell Reports: Control of bacterial virulence through the peptide signature of the habitat

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

New ISB Article by Erik Johansson et al in Nature Communications

Professor Erik Johansson has published an article in Nature Communications named “Structural consequence of the most frequently recurring cancer-associated substitution in DNA polymerase epsilon“. The study was a collaboration with Uppsala University and University of Nebraska Medical Center. The article can be found at: “”

Magnus Wolf-Watz named professor

Magnus Wolf-Watz was named professor in biophysical chemistry on May 1:st 2018.