Research

Research

The IP3 3-kinase is capable of binding and phosphorylating various analogs of its substrate, IP3, thus demonstrating new biosynthetic capabilities. This discovery opens new perspectives in the field of drug design.

The study identifies a LD-transpeptidase from Gluconobacter oxydans, LDTGo, capable of generating 1,3 cross-links in the peptidoglycan. A high-resolution structure has been determined, revealing distinctive features.

These structures are not forgotten due to lack of interest but rather because they are difficult to study. Until now, there has been only one published structure of an antiparallel triplex, and that was 30 years ago.

We provide the first experimental analysis of AGT structural dynamics, showing that stability is heterogeneous in the native state and providing a blueprint for frustrated regions with potentially functional relevance.