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TitleConformational landscape of the mycobacterial inosine 5'-monophosphate dehydrogenase octamerization interface.
Journal, issue, pagesJ Struct Biol, Vol. 217, Issue 2, Page 108198, Year 2025
Publish dateMar 17, 2025
AuthorsOndřej Bulvas / Zdeněk Knejzlík / Anatolij Filimoněnko / Tomáš Kouba / Iva Pichová /
PubMed AbstractInosine 5'-monophosphate dehydrogenase (IMPDH), a key enzyme in bacterial purine metabolism, plays an essential role in the biosynthesis of guanine nucleotides and shows promise as a target for ...Inosine 5'-monophosphate dehydrogenase (IMPDH), a key enzyme in bacterial purine metabolism, plays an essential role in the biosynthesis of guanine nucleotides and shows promise as a target for antimicrobial drug development. Despite its significance, the conformational dynamics and substrate-induced structural changes in bacterial IMPDH remain poorly understood, particularly with respect to its octameric assembly. Using cryo-EM, we present full-length structures of IMPDH from Mycobacterium smegmatis (MsmIMPDH) captured in a reaction intermediate state, revealing conformational changes upon substrate binding. The structures feature resolved flexible loops that coordinate the binding of the substrate, the cofactor, and the K ion. Our structural analysis identifies a novel octamerization interface unique to MsmIMPDH. Additionally, a previously unobserved barrel-like density suggests potential self-interactions within the C-terminal regions, hinting at a regulatory mechanism tied to assembly and function of the enzyme. These data provide insights into substrate-induced conformational dynamics and novel interaction interfaces in MsmIMPDH, potentially informing the development of IMPDH-targeted drugs.
External linksJ Struct Biol / PubMed:40107326
MethodsEM (single particle)
Resolution2.39 - 3.01 Å
Structure data

52559

9i0k

EMDB-52559, PDB-9i0k:
Mycobacterium smegmatis inosine monophosphate dehydrogenase (IMPDH) E-XMP* intermediate, compressed
Method: EM (single particle) / Resolution: 2.73 Å

52560

9i0l

EMDB-52560, PDB-9i0l:
Mycobacterium smegmatis inosine monophosphate dehydrogenase (IMPDH) E-XMP* intermediate, extended
Method: EM (single particle) / Resolution: 2.39 Å

52561

9i0m

EMDB-52561, PDB-9i0m:
Mycobacterium smegmatis inosine monophosphate dehydrogenase (IMPDH) saturating ATP+IMP-bound form, extended
Method: EM (single particle) / Resolution: 3.01 Å

Chemicals

ChemComp-IMP:
INOSINIC ACID

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsOXIDOREDUCTASE / Octamer / reaction intermediate / Purine metabolism / IMPDH / ligand complex

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