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TitleStructural and kinetic analysis of distinct active and inactive states of Burkholderia cenocepacia orotate phosphoribosyltransferase.
Journal, issue, pagesArch Biochem Biophys, Vol. 766, Page 110332, Year 2025
Publish dateFeb 10, 2025
AuthorsNandini Sharma / Zachary R Turlington / Sean P Zupko / Michael N Catoggio / Christine M Lukacs / Dmitry Serbzhinskiy / Jan Abendroth / Thomas E Edwards / Donald D Lorimer / George Barrera / Sydney Willis / Olive Beyer / Sarah Toay / Teng Da Li / Andrew T Torelli / Katherine A Hicks / Jarrod B French /
PubMed AbstractOrotate phosphoribosyltransferase (OPRT) catalyzes the reaction that adds the pyrimidine base to the ribose in the penultimate step of the de novo biosynthesis of pyrimidine nucleotides. The OPRT ...Orotate phosphoribosyltransferase (OPRT) catalyzes the reaction that adds the pyrimidine base to the ribose in the penultimate step of the de novo biosynthesis of pyrimidine nucleotides. The OPRT structure consists of an obligate dimer, conserved throughout the phosphoribosyltransferase family. Here, we describe the structural characterization of Burkholderia cenocepacia OPRT (BcOPRT), both by X-ray crystallography and Cryo electron microscopy (Cryo-EM). While the known dimer is present in the structure of BcOPRT, a putative hexameric form was also observed by multiple methods. Analyses by chromatography, Cryo-EM, and kinetics indicate that both dimeric and hexameric forms of this enzyme are present together in solution. Comparison of the kinetics of the native protein and two variants, which were specifically designed to prevent hexamerization, reveal that only the hexameric form is enzymatically active. Collectively, these data suggest that BcOPRT may use oligomerization to control overall enzymatic activity, thus contributing to the local regulation of pyrimidine biosynthesis in this organism.
External linksArch Biochem Biophys / PubMed:39938730 / PubMed Central
MethodsEM (single particle)
Resolution3.07 Å
Structure data

47526

9e5g

EMDB-47526, PDB-9e5g:
Cryo-EM structure of Burkholderia cenocepacia orotate phosphoribosyltransferase
Method: EM (single particle) / Resolution: 3.07 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • burkholderia cenocepacia j2315 (bacteria)
KeywordsTRANSFERASE / orotic acid phosphoribosyltransferase

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