Insight into the role of the Bateman domain at the molecular and physiological levels through engineered IMP dehydrogenases.

Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE

Publication: 2001- : Woodbury, NY : Cold Spring Harbor Laboratory Press
Original Publication: New York, N.Y. : Cambridge University Press, c1992-

IMP Dehydrogenase*/genetics ; IMP Dehydrogenase*/metabolism ; Adenosine Triphosphate*; Bacteria/metabolism ; Inosine

Inosine 5'-monophosphate (IMP) dehydrogenase (IMPDH) is an 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 cause 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.
(© 2023 The Protein Society.)

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Keywords: Bateman domain; IMPDH; allostery; enzymology; integrative structural biology; purine nucleotide biosynthesis; quaternary structure; structure-function relationship

EC 1.1.1.205 (IMP Dehydrogenase)
8L70Q75FXE (Adenosine Triphosphate)
5A614L51CT (Inosine)

Date Created: 20230620 Date Completed: 20230731 Latest Revision: 20240802

20240802

PMC10357500

10.1002/pro.4703

37338125