9vlf

Structural studies on the conformation changes induced by ligand binding in an Adenine phosphoribosyltransferase (FnAPRT) from Fusobacterium nucleatum

spinqualitylabelsall models 9vlf, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9vlf is a 1 chain structure with sequence from Fusobacterium nucleatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.61Å Ligands: AMP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APT_FUSNN Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. Publication Abstract from PubMed BACKGROUND: Adenine phosphoribosyltransferase (APRT) is an enzyme that facilitates adenosine monophosphate (AMP) biosynthesis by transferring a phosphoribosyl group to adenine using phosphoribosyl pyrophosphate as a donor. While the human enzyme is well characterized, structural insights into bacterial APRTs remain limited. Fusobacterium nucleatum is associated with periodontal disease, yet its APRT enzyme (FnAPRT) has not been structurally investigated. OBJECTIVE: This study aimed to examine the crystal structure of FnAPRT and ligand-induced conformational changes to understand its enzymatic and substrate recognition mechanisms. METHODS: The FnAPRT protein was heterologously expressed in Escherichia coli, followed by initial purification using nickel-charged affinity resin chromatography and further purification through size-exclusion chromatography. The FnAPRT structure was resolved using X-ray crystallography and compared with that of E. coli APRT (EcAPRT), exhibiting the highest amino acid sequence similarity among bacterial APRT structures. RESULTS: AMP and phosphate (PO4) were observed in the active site of FnAPRT. Significant differences in ligand positioning were observed between the AMP-PO4-bound structures of FnAPRT and EcAPRT. Structural shifts induced by AMP-PO4 binding were detected. The Arg78 and Lys82 residues from the alternate subunit occupied the PO4 site in the absence of ligands, but they interacted with PO4 upon AMP-PO4 binding. Structural comparison of the AMP-PO(4)-bound FnAPRT with that of the adenine-bound EcAPRT highlighted variations in the adenine-binding site and associated structural changes. DISCUSSION: Structural comparison of the AMP-PO4-bound FnAPRT with that of the adeninebound EcAPRT highlighted variations in the adenine-binding site and the associated structural changes. CONCLUSION: The AMP-PO(4)-bound FnAPRT exhibited distinct ligand-binding modes despite sharing a high sequence similarity with EcAPRT. The structures demonstrated ligand movement during bacterial APRT reactions. Structural Insights into Ligand-Induced Conformational Changes in Adenine Phosphoribosyl Transferase from Fusobacterium nucleatum.,Kim B, Hwang J, Do H, Shim YS, Lee JH Protein Pept Lett. 2026 Jan 22. doi: 10.2174/0109298665403166251021110505. PMID:41588988 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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