ArticleNature2015
Structural insights into the bacterial carbon-phosphorus lyase machinery.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed.
- Impact of the Fenton pretreatment on enhanced biological phosphorus removal: emphasizing variations in microbial community and metabolism.Biodegradation · 2026Article
- Phosphate-solubilizing bacteria: a review of diversity, mechanisms, and applications in sustainable agriculture.Frontiers in microbiology · 2026Review
- Unveiling Crocosphaera Responses to Phosphorus Depletion: Insights From Genome Analysis and Functional Characterization.Environmental microbiology · 2025Article
- Phylogenetic analysis of microbial CP-lyase cluster genes for bioremediation of phosphonate.AMB Express · 2025Article
- The functional mechanisms of phosphite and its applications in crop plants.Frontiers in plant science · 2025Review
- Integrating AlphaFold pLDDT Scores into CABS-flex for enhanced protein flexibility simulations.Computational and structural biotechnology journal · 2024Article
- Disentangling the Regulatory Response ofACS synthetic biology · 2024Article
- Investigating eukaryotic and prokaryotic diversity and functional potential in the cold and alkaline ikaite columns in Greenland.Frontiers in microbiology · 2024Article
- Proteomic response to phosphorus deficiency and aluminum stress of three aluminum-tolerant phosphobacteria isolated from acidic soils.iScience · 2023Article
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
- Engineering Escherichia coli to Utilize Erythritol as Sole Carbon Source.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Stille type P-C coupling polycondensation towards phosphorus-crosslinked polythiophenes with P-regulated photocatalytic hydrogen evolution.Chemical science · 2023Article
- Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.Nature communications · 2023Article
- Global and seasonal variation of marine phosphonate metabolism.The ISME journal · 2022Article
- PCycDB: a comprehensive and accurate database for fast analysis of phosphorus cycling genes.Microbiome · 2022Article
- Rhodium-catalyzed selective direct arylation of phosphines with aryl bromides.Nature communications · 2022Article
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- A genomic view of trophic and metabolic diversity in clade-specific Lamellodysidea sponge microbiomes.Microbiome · 2020Article
- Phosphite binding by the HtxB periplasmic binding protein depends on the protonation state of the ligand.Scientific reports · 2019Article
- Phosphate-limited ocean regions select for bacterial populations enriched in the carbon-phosphorus lyase pathway for phosphonate degradation.Environmental microbiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Phosphorus is required for all life and microorganisms can extract it from their environment through several metabolic pathways. When phosphate is in limited supply, some bacteria are able to use phosphonate compounds, which require specialized enzymatic machinery to break the stable carbon-phosphorus (C-P) bond. Despite its importance, the details of how this machinery catabolizes phosphonates remain unknown. Here we determine the crystal structure of the 240-kilodalton Escherichia coli C-P lyase core complex (PhnG-PhnH-PhnI-PhnJ; PhnGHIJ), and show that it is a two-fold symmetric hetero-octamer comprising an intertwined network of subunits with unexpected self-homologies. It contains two potential active sites that probably couple phosphonate compounds to ATP and subsequently hydrolyse the C-P bond. We map the binding site of PhnK on the complex using electron microscopy, and show that it binds to a conserved insertion domain of PhnJ. Our results provide a structural basis for understanding microbial phosphonate breakdown.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.