9t9o

Crystal structure of Ap4A Hydrolase (ApaH) from Pseudomonas aeruginosa in complex with Mn ions

spinqualitylabelsall models 9t9o, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9t9o is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: CL, MG, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APAH_PSEAE Hydrolyzes diadenosine 5',5-P1,P4-tetraphosphate to yield ADP. Publication Abstract from PubMed Infections by Pseudomonas aeruginosa are a major cause of severe morbidity and mortality in immunocompromised patients and people with cystic fibrosis, largely due to the pathogen's ability to resist antibiotic treatment and to deploy multiple virulence strategies that promote persistence in the host. We have recently uncovered that the signaling molecule diadenosine tetraphosphate (Ap4A) acts as a crucial regulator of P. aeruginosa virulence. Specifically, deletion of the Ap4A-degrading enzyme, diadenosine tetraphosphatase (ApaH), dramatically reduces the expression of key virulence factors. The structural and molecular properties of P. aeruginosa ApaH (PaApaH) remain uncharacterized. Here, we present an integrated biochemical, structural, computational, and phenotypic characterization of PaApaH. We define the molecular determinants of its manganese-dependent Ap4A hydrolytic mechanism and establish a direct functional link between PaApaH catalytic activity and virulence phenotypes in vivo. Together with the absence of ApaH homologs in eukaryotes, these findings place PaApaH as an attractive and selective target for antivirulence therapeutic strategies against P. aeruginosa infections. Structural and functional insights into Pseudomonas aeruginosa ApaH, a diadenosine tetraphosphatase crucial for bacterial virulence.,Pistoia G, Cervoni M, Catalano F, Troilo F, Guidi F, Comparini E, Mignogna G, Travaglini-Allocatelli C, Giuffre A, Coluccia A, Imperi F, Di Matteo A, Giardina G Protein Sci. 2026 Sep;35(9):e70781. doi: 10.1002/pro.70781. PMID:42640267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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