Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components

Olivier Genest1, Meina Neumann, Farida Seduk

  • 1Laboratoire de Chimie Bactérienne, Institut de Biologie Structurale et Microbiologie-CNRS, 31 chemin Joseph Aiguier, Marseille cedex 20, France.

Summary

The TorD chaperone is crucial for molybdenum enzyme maturation, binding both the cofactor and its precursor. This interaction facilitates the insertion of the molybdenum cofactor into the TorA enzyme.

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