Structural insights into the bacterial carbon - phosphorus lyase machinery

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Paulina Seweryn, Denmark
  • Lan Bich Van
  • Morten Kjeldgaard
  • Christoffer J. Russo, Medical Research Council Laboratory of Molecular Biology, United Kingdom
  • Lori A. Passmore, Medical Research Council Laboratory of Molecular Biology, United Kingdom
  • Bjarne Hove-Jensen, Denmark
  • Bjarne Jochimsen
  • ,
  • Ditlev E. Brodersen
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.
Original languageEnglish
JournalNature
Volume525
Pages (from-to)68-72
Number of pages5
ISSN0028-0836
DOIs
Publication statusPublished - Sep 2015

See relations at Aarhus University Citationformats

Activities

  • Gordon Research Conference

    Activity: Participating in or organising an event typesParticipation in or organisation af a conference

ID: 90616073