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9FPE

Wild type Purine Nucleoside Phosphorylase from E.coli in complex with N2,3-etheno-2-aminopurine

This is a non-PDB format compatible entry.
Summary for 9FPE
Entry DOI10.2210/pdb9fpe/pdb
DescriptorPurine nucleoside phosphorylase DeoD-type, GLYCEROL, N,2,3-etheno-2-aminopurine, ... (6 entities in total)
Functional Keywordsfluorescent ligand, transferase
Biological sourceEscherichia coli K-12
Total number of polymer chains3
Total formula weight79272.67
Authors
Narczyk, M.,Krystian, M.,Stachelska-Wierzchowska, A.,Wierzchowski, J. (deposition date: 2024-06-13, release date: 2024-10-30)
Primary citationStachelska-Wierzchowska, A.,Narczyk, M.,Wierzchowski, J.,Bzowska, A.,Wielgus-Kutrowska, B.
Interaction of Tri-Cyclic Nucleobase Analogs with Enzymes of Purine Metabolism: Xanthine Oxidase and Purine Nucleoside Phosphorylase.
Int J Mol Sci, 25:-, 2024
Cited by
PubMed Abstract: Fluorescent markers play important roles in spectroscopic and microscopic research techniques and are broadly used in basic and applied sciences. We have obtained markers with fluorescent properties, two etheno derivatives of 2-aminopurine, as follows: 1,N-etheno-2-aminopurine (1,N-ε2APu, ) and N,3-etheno-2-aminopurine (N,3-ε2APu, ). In the present paper, we investigate their interaction with two key enzymes of purine metabolism, purine nucleoside phosphorylase (PNP), and xanthine oxidase (XO), using diffraction of X-rays on protein crystals, isothermal titration calorimetry, and fluorescence spectroscopy. Crystals were obtained and structures were solved for WT PNP and D204N-PNP mutant in a complex with N,3-ε2APu (). In the case of WT PNP-1,N-ε2APu () complex, the electron density corresponding to the ligand could not be identified in the active site. Small electron density bobbles may indicate that the ligand binds to the active site of a small number of molecules. On the basis of spectroscopic studies in solution, we found that, in contrast to PNP, 1,N-ε2APu () is the ligand with better affinity to XO. Enzymatic oxidation of () leads to a marked increase in fluorescence near 400 nm. Hence, we have developed a new method to determine XO activity in biological material, particularly suitable for milk analysis.
PubMed: 39408755
DOI: 10.3390/ijms251910426
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.35 Å)
Structure validation

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数据于2025-10-08公开中

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