Entries by Magnus Wolf-Watz

PhD position in human protein kinases

 A PhD position in biochemistry is available in the laboratory of Professor Magnus Wolf-Watz at the Department of Chemistry, Umeå University, Sweden. The PhD project is aimed at uncovering novel molecular mechanisms underlying the function of human protein kinases. Focus will be on two specific protein kinases that are intimately linked to a number of […]

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.  https://www.pnas.org/content/116/32/15924.long

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 […]

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 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: “www.nature.com/articles/s41467-018-08114-9”

New Integrated Structural Biology article: “Formation of a translocation competent protein complex by a dynamic wrap-around binding mechanism.”

This paper from the Wolf-Watz lab describes the discovery of a fundamentally new mechanism underlying protein-protein interactions. The chaperone-binding domain of the Yersinia effector protein YopH was found to lose its globular structure upon formation of a wrap-around architecture with its chaperone SycH. The mechanism is best described as a coupled binding and disordering event. […]