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Cooperative Allosteric Transitions01:58

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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Uncoupling conformational states from activity in an allosteric enzyme.

João P Pisco1, Cesira de Chiara1, Kamila J Pacholarz2

  • 1Mycobacterial Metabolism and Antibiotic Research Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

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Researchers identified 3-(2-thienyl)-L-alanine (TIH) as an activator for ATP-phosphoribosyltransferase (ATP-PRT). The study reveals that enzyme conformation and function are uncoupled, highlighting the role of dynamic processes in allosteric regulation.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • ATP-phosphoribosyltransferase (ATP-PRT) exists in equilibrium between open (active) and closed (inhibited) conformations.
  • The precise structure-function relationship of ATP-PRT allosteric regulation remains incompletely understood.

Purpose of the Study:

  • To develop a screening strategy for ATP-PRT modulators.
  • To identify novel allosteric activators and characterize their mechanism of action.

Main Methods:

  • Enzyme activity screening and kinetic analysis.
  • X-ray crystallography.
  • Native ion-mobility mass spectrometry.

Main Results:

  • 3-(2-thienyl)-L-alanine (TIH) was identified as an allosteric activator of ATP-PRT.
  • Kinetic studies showed co-occupancy of allosteric sites by TIH and L-histidine.
  • Structural and mass spectrometry data revealed that the TIH-bound active state resembles the L-histidine-bound closed conformation, uncoupling conformation from function.

Conclusions:

  • Allosteric regulation of ATP-PRT is driven by dynamic processes rather than distinct conformational states.
  • The findings suggest that dynamic mechanisms may govern other enzymes with ferredoxin-like allosteric domains.