Daniel Frey

TL;DR: The findings define the molecular basis of CAP-Gly domain function, including the tubulin detyrosination-tyrosination cycle, and establish fundamental roles for the interaction between CAP-gly proteins and C-terminal EEY/F sequence motifs in regulating complex and dynamic cellular processes.

TL;DR: Structural analysis of a complex of tubulin and tubulin tyrosine ligase (TTL) reveals insights into TTL’s enzymatic mechanism, how it discriminates between α- and β-tubulin, and its possible evolutionary origin.

TL;DR: The high-resolution crystal structure of the BoNT/A receptor-binding domain (BoNT/ a-RBD) in complex with the SV2C luminal domain (SV2C-LD) is determined, providing a strong platform for the development of novel antitoxin agents and for the rational design of Bo NT/A variants with improved therapeutic properties.

TL;DR: Acembl is introduced, a versatile and automatable system for protein-complex expression in Escherichia coli that uses recombineering to facilitate multigene assembly and diversification.

TL;DR: This work brings together crystallographic, biophysical, and reconstitution assays to demonstrate that the human centriolar protein CPAP binds and “caps” microtubule plus ends by associating with a site of β-tubulin engaged in longitudinal tubulin- Tubulin interactions.