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Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target
Sarah C Atkinson1, Con Dogovski2, Kathleen Wood3
1Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, 30 Flemington Road, University of Melbourne, Parkville, VIC 3010, Australia.
Structure (London, England : 1993)
|May 29, 2018
Summary
Substrate pyruvate stabilizes the active tetrameric form of Clostridium botulinum dihydrodipicolinate synthase. New protein dynamics-mass spectrometry (ProD-MS) reveals how ligands stabilize multimeric enzymes.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Protein dynamics and structural flexibility are crucial for biological molecule function.
- Clostridium botulinum dihydrodipicolinate synthase is a key antibiotic target enzyme.
Purpose of the Study:
- To investigate substrate-mediated changes in protein flexibility.
- To understand how pyruvate binding affects the enzyme's structure and activity.
Main Methods:
- X-ray crystallography (apo and substrate-bound states).
- Neutron and small-angle X-ray scattering (SAXS).
- Protein dynamics-mass spectrometry (ProD-MS).
- Analytical ultracentrifugation.
Main Results:
- Pyruvate stabilizes the active dimer-of-dimers (tetrameric) form of the enzyme.
- Crystal structures showed minimal differences between apo and substrate-bound states.
- ProD-MS revealed pyruvate locks the dimer conformation, promoting tetramer formation.
Conclusions:
- Ligand binding can stabilize multimeric enzyme complexes through conformational locking.
- ProD-MS is a valuable technique for studying protein dynamics.
- Understanding these dynamics provides insight into enzyme regulation and drug development.
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