ArticleStructure (London, England : 1993)2016
Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Bacterial community succession and functional gene dynamics of nitrogen and phosphorus cycling in recirculating aquaculture systems of shrimp.FEMS microbiology ecology · 2026Article
- Phylogenetic analysis of microbial CP-lyase cluster genes for bioremediation of phosphonate.AMB Express · 2025Article
- The transcriptome response of Enterobacter sp. S-33 is modulated by low pH-stress.Genes & genomics · 2024Article
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
- Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.Nature communications · 2023Article
- Strategies for the Biodegradation of Polyfluorinated Compounds.Microorganisms · 2022Review
- Guidelines for using Bsoft for high resolution reconstruction and validation of biomolecular structures from electron micrographs.Protein science : a publication of the Protein Society · 2018Article
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Abstract
The carbon-phosphorus (C-P) lyase complex is essential for the metabolism of unactivated phosphonates to phosphate in bacteria. Using single-particle cryo-electron microscopy, we determined two structures of the C-P lyase core complex PhnG2H2I2J2, with or without PhnK. PhnG2H2I2J2 is a two-fold symmetric hetero-octamer. Its two PhnJ subunits provide two identical binding sites for PhnK. Only one PhnK binds to PhnG2H2I2J2 due to steric hindrance. PhnK is homologous to the nucleotide-binding domain (NBD) of ATP-binding cassette transporters. The α helices 3 and 4 of PhnK bind to α helix 6 and a loop (residues 227-230) of PhnJ, in a different mode from the binding of NBDs to their transmembrane partners. Moreover, binding of PhnK exposes the active site residue, Gly32 of PhnJ, located near the interface between PhnJ and PhnH. This structural information provides a basis for further deciphering of the reaction mechanism of the C-P lyase.
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