We use X-ray crystallography to obtain high resolution information on the mechanisms of Ub recognition, and interpretation of Ub signals.
A unique tool developed in our lab allows us to purify ubiquitylated-protein in milligram quantities sufficient for crystallization (to learn more see highlight in Nature Methods 2012; or read our EMBO J paper 2012).
Recently we determined the crystal structure of the proteasomal Ub receptor Rpn10 in its ubiquitylated state.
The structure uncovered a novel Ub-binding domain within the receptor and provided structural information that explains how self-ubiquitylation is directed to a specific lysine residue (K84). Moreover, the structure shows that Rpn10 self-ubiquitylation dissociate the modified Rpn10 (Ub-Rpn10) from the proteasome (Nature Communication 2016).
We also determined the crystal structure of a novel Ub-binding domains (ENTH domains from Epsin-1 of yeast and zebrafish). These domains shows ultraweak affinity to Ub. We employed our bacterial genetic selection system to characterize the ENTH:Ub interface (Nature Methods 2016)
We share a rotating anode Rigaku X-ray machine.
To obtain phases and high resolution data, students tarvel to the European Synchrotron Radiation Facility (ESRF) at Grenoble, France.