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  • nrc
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  • Clinical Research Nurse
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  • PhD Student
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  • Research Engineer
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  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
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Published in Protein science : a publication of the Protein Society - 20 Jun 2023

Gedeon A, Ayoub N, Brûlé S, Raynal B, Karimova G, Gelin M, Mechaly A, Haouz A, Labesse G, Munier-Lehmann H

Link to Pubmed [PMID] – 37338125

Link to DOI – 10.1002/pro.4703

Protein Sci 2023 Jun; (): e4703

Inosine 5′-monophosphate dehydrogenase (IMPDH) is a^ ubiquitous enzyme that catalyzes the NAD+ -dependent oxidation of inosine 5′-monophosphate into xanthosine 5′-monophosphate. This enzyme is formed of two distinct domains, a core domain where the catalytic reaction occurs, and a less-conserved Bateman domain. Our previous studies gave rise to the classification of bacterial IMPDHs into two classes, according to their oligomeric and kinetic properties. MgATP is a common effector but leading to different effects when it binds within the Bateman domain: it is either an allosteric activator for class I IMPDHs or a modulator of the oligomeric state for class II IMPDHs.To get insight into the role of the Bateman domain in the dissimilar properties of the two classes, deleted variants of the Bateman domain and chimeras issued from the interchange of the Bateman domain between the three selected IMPDHs have been generated and characterized using an integrative structural biology approach. Biochemical, biophysical, structural and physiological studies of these variants unveil the Bateman domain as being the carrier of the molecular behaviors of both classes. This article is protected by copyright. All rights reserved.