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RSS FeedsSubstrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target (Structure)

 
 

25 may 2018 06:01:26

 
Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target (Structure)
 


Atkinson et al. show that pyruvate binding locks the conformation of the C. botulinum DHDPS dimer that promotes tetramerization. They describe a new method (ProD-MS) that assesses protein dynamics on a slow (second-minute) timescale.


 
86 viewsCategory: Biochemistry
 
Topology and Oligomerization of Mono- and Oligomeric Proteins Regulate Their Half-Lives in the Cell (Structure)
Mis16 Switches Function from a Histone H4 Chaperone to a CENP-ACnp1-Specific Assembly Factor through Eic1 Interaction (Structure)
 
 
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