4XB6

Structure of the E. coli C-P lyase core complex

Summary for 4XB6

• Entry DOI: 10.2210/pdb4xb6/pdb
• Descriptor: Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH, Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI, ... (7 entities in total)
• Functional Keywords: protein complex, transferase
• Biological source: Escherichia coli str. K-12 substr. MG1655; More
• Total number of polymer chains: 8
• Total formula weight: 217823.76

Authors

Brodersen, D.E. (deposition date: 2014-12-16, release date: 2015-08-19, Last modification date: 2024-11-20)

Primary citation

Seweryn, P.,Van, L.B.,Kjeldgaard, M.,Russo, C.J.,Passmore, L.A.,Hove-Jensen, B.,Jochimsen, B.,Brodersen, D.E.
Structural insights into the bacterial carbon-phosphorus lyase machinery.
Nature, 525:68-72, 2015

PubMed 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.

PubMed: 26280334
DOI: 10.1038/nature14683

Experimental method

X-RAY DIFFRACTION (1.7 Å)