ArticleIUCrJ2014
The structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like fold.
Article in IUCrJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Analysis and characterization of a novel metallophosphoesterase fromBiochemistry and biophysics reports · 2026Article
- Selective isotope labeling probes the chemical capacity and reaction mechanism of a heterobimetallic Mn/Fe protein.Journal of inorganic biochemistry · 2025Article
- Nematode-resistance loci in upland cotton genomes are associated with structural differences.G3 (Bethesda, Md.) · 2024Article
- Purple acid phosphatases: roles in phosphate utilization and new emerging functions.Plant cell reports · 2022Review
- Overlapping Functions of the Paralogous Proteins AtPAP2 and AtPAP9 inInternational journal of molecular sciences · 2021Article
- Fungal Endophyte Colonization Patterns Alter Over Time in the Novel Association BetweenFrontiers in plant science · 2020Article
- Guanidine- and purine-functionalized ligands of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Identification of Tea Plant Purple Acid Phosphatase Genes and Their Expression Responses to Excess Iron.International journal of molecular sciences · 2019Article
- Article
- Characterization of the Catalytic Structure of Plant Phytase, Protein Tyrosine Phosphatase-Like Phytase, and Histidine Acid Phytases and Their Biotechnological Applications.Enzyme research · 2018Review
- QTL-seq approach identified genomic regions and diagnostic markers for rust and late leaf spot resistance in groundnut (Arachis hypogaea L.).Plant biotechnology journal · 2017Article
- AtPAP2 modulates the import of the small subunit of Rubisco into chloroplasts.Plant signaling & behavior · 2016Article
- A purple acid phosphatase plays a role in nodule formation and nitrogen fixation in Astragalus sinicus.Plant molecular biology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatases function in the production, transport and recycling of inorganic phosphorus, which is crucial for cellular metabolism and bioenergetics, as well as in bacterial killing, since they are able to generate reactive oxygen species via Fenton chemistry. Diphosphonucleotide phosphatase/phosphodiesterase (PPD1), a glycoprotein plant purple acid phosphatase (PAP) from yellow lupin seeds, contains a bimetallic Fe-Mn catalytic site which is most active at acidic pH. Unlike other plant PAPs, PPD1 cleaves the pyrophosphate bond in diphosphonucleotides and the phosphodiester bond in various phosphodiesters. The homohexameric organization of PPD1, as revealed by a 1.65 Å resolution crystal structure and confirmed by solution X-ray scattering, is unique among plant PAPs, for which only homodimers have previously been reported. A phosphate anion is bound in a bidentate fashion at the active site, bridging the Fe and Mn atoms in a binding mode similar to that previously reported for sweet potato PAP, which suggests that common features occur in their catalytic mechanisms. The N-terminal domain of PPD1 has an unexpected and unique fibronectin type III-like fold that is absent in other plant PAPs. Here, the in vitro DNA-cleavage activity of PPD1 is demonstrated and it is proposed that the fibronectin III-like domain, which 'overhangs' the active site, is involved in DNA selectivity, binding and activation. The degradation of DNA by PPD1 implies a role for PPD1 in plant growth and repair and in pathogen defence.
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