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Updated: Jul 4, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
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.
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.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Molybdenum-containing enzymes require complex cofactor insertion for activity.
- The maturation of trimethylamine-oxide reductase (TorA) depends on a specific chaperone, TorD.
Purpose of the Study:
- To elucidate the role of TorD in TorA maturation.
- To investigate TorD's interactions with apo-TorA, cofactor biosynthesis components, and the molybdenum cofactor.
Main Methods:
- Random mutagenesis of TorD to identify key functional regions.
- Biochemical assays to study protein-protein interactions.
- Analysis of TorD binding to different forms of the molybdenum cofactor.
Main Results:
- Alpha-helix 5 of TorD is essential for binding the apo-TorA core, driving TorA maturation.
- TorD interacts with MobA and Mo-molybdopterin, key components in molybdenum cofactor biosynthesis.
- TorD binds both precursor and mature forms of the molybdenum cofactor (molybdopterin-guanine dinucleotide).
Conclusions:
- TorD acts as a central platform connecting molybdenum cofactor synthesis and its insertion into TorA.
- TorD's interaction with alpha-helix 5 is critical for recruiting the apo-TorA core.
- TorD coordinates the final steps of cofactor maturation and delivery to the target enzyme.
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