A concise strategy for engineering functional, supramolecular protein complexes has now been developed based on single-mutation-mediated covalent tethering. Metalloproteins designed with this method can sustain large alterations to the metal coordination environment, bind small molecules, exhibit reversible redox activity and sustain large alterations to the protein structure.

Shape transformation of proteins created by design in the laboratory is challenging. Here, the authors present a disulfide-mediated approach for the preparation of 16-mer, 24-mer, and 48-mer nanocages from an 8-mer bowl-like protein building block.

A method combining genetic-code expansion, bioorthogonal Staudinger reduction and sortase-mediated transpeptidation enables site-specific and orthogonal modification of proteins with ubiquitin and SUMO in vitro and in living cells.

Dennis Eickelbeck et al. engineered light-activated constructs, CaMello and CaMello-5HT_2A, which are targeted to the 5HT_2A-R domains and enable visualization of calcium signals and receptor trafficking in response to activation. The reported CaMello tool could be applied to other GPCRs coupled to the G_q/11 signaling pathways which may shed light on mechanisms of GPCR localization and plasticity.