The Swedish Research Council has decided to award a 25.2 MSEK grant to a coalition of research groups at Umeå University and the University of Helsinki within the call “Research environment grant within infection and antibiotics”.

The project “Multimodal imaging and proteomics to study flavivirus replication and molecular disease mechanisms” is headed by flavivirologist Anna Överby Wernstedt at Umeå University and includes the biostruct-affiliated group of Lars-Anders Carlson. The other two teams involved in the collaboration are the Umeå-based group of Richard Lundmark and the Helsinki-based group of Sarah Butcher.

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. The finding was enabled by an integrated structural biology approach by a five-lab effort and centered on NMR, SAXS and computational chemistry.

The article is published in Journal of Molecular Biology (2018), 430, 3157.

Kulén M, Lindgren M, Hansen S, Cairns AG, Grundström C, Begum A, van der Lingen I, Brännström K, Hall M, Sauer UH, Johansson J, Sauer-Eriksson AE, Almqvist F. J Med Chem. 2018 May 10;61(9):4165-4175.