Abstract
Phosphonate compounds act as a nutrient source for some microorganisms when phosphate is limiting but require a specialised enzymatic machinery due to the presence of the highly stable carbon-phosphorus bond. Despite the fundamental importance to microbial metabolism, the details of how the proteins encoded in the phn operon act in concert to catabolise phosphonate remain unknown. We have determined the crystal structure of a 240 kDa Escherichia coli carbon-phosphorus lyase core complex at 1.7 Å and show that it comprises a highly intertwined network of subunits with several unexpected structural features. The complex contains at least two different active sites and suggest a revision of current models of carbon-phosphorus bond cleavage. Using electron microscopy, we map the binding site of an additional protein subunit, which may use ATP for driving conformational changes during the reaction. Our results delineate the overall architecture of the carbon-phosphorus lyase machinery and give detailed insight into the mechanism underlying microbial phosphonate breakdown.
| Original language | English |
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| Publication date | 12 Jul 2015 |
| Number of pages | 1 |
| Publication status | Published - 12 Jul 2015 |
| Event | Gordon Research Conference: Enzymes, Coenzymes & Metabolic Pathways - Waterville Valley Resort, Waterville Valley, NH, United States Duration: 12 Jul 2015 → 17 Jul 2015 |
Conference
| Conference | Gordon Research Conference |
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| Location | Waterville Valley Resort |
| Country/Territory | United States |
| City | Waterville Valley, NH |
| Period | 12/07/2015 → 17/07/2015 |