ArticleNature communications2023
Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Contrasting microbial iron metabolism in sediments from oxic and hypoxic estuaries.Frontiers in microbiology · 2026Article
- Diverse marineMarine life science & technology · 2025Article
- Unveiling Crocosphaera Responses to Phosphorus Depletion: Insights From Genome Analysis and Functional Characterization.Environmental microbiology · 2025Article
- Article
- Proteomic evidence for aerobic methane production in groundwater by methylotrophic Methylotenera.The ISME journal · 2025Article
- Disentangling the Regulatory Response ofACS synthetic biology · 2024Article
- Genome-wide comparative analysis of clinical and environmental strains of the opportunistic pathogenFrontiers in microbiology · 2024Article
- Correlation of methane production with physiological traits inFrontiers in microbiology · 2024Article
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, the 14-cistron phn operon encoding carbon-phosphorus lyase allows for utilisation of phosphorus from a wide range of stable phosphonate compounds containing a C-P bond. As part of a complex, multi-step pathway, the PhnJ subunit was shown to cleave the C-P bond via a radical mechanism, however, the details of the reaction could not immediately be reconciled with the crystal structure of a 220 kDa PhnGHIJ C-P lyase core complex, leaving a significant gap in our understanding of phosphonate breakdown in bacteria. Here, we show using single-particle cryogenic electron microscopy that PhnJ mediates binding of a double dimer of the ATP-binding cassette proteins, PhnK and PhnL, to the core complex. ATP hydrolysis induces drastic structural remodelling leading to opening of the core complex and reconfiguration of a metal-binding and putative active site located at the interface between the PhnI and PhnJ subunits.
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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.