+検索条件
-Structure paper
タイトル | Structural insights into the bacterial carbon-phosphorus lyase machinery. |
---|---|
ジャーナル・号・ページ | Nature, Vol. 525, Issue 7567, Page 68-72, Year 2015 |
掲載日 | 2015年9月3日 |
著者 | Paulina Seweryn / Lan Bich Van / Morten Kjeldgaard / Christopher J Russo / Lori A Passmore / Bjarne Hove-Jensen / Bjarne Jochimsen / Ditlev E Brodersen / |
PubMed 要旨 | 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 ...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. |
リンク | Nature / PubMed:26280334 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.7 - 16.0 Å |
構造データ | EMDB-3033: PDB-4xb6: |
化合物 | ChemComp-SO4: ChemComp-ZN: ChemComp-HOH: |
由来 |
|
キーワード | TRANSFERASE (転移酵素) / protein complex (タンパク質複合体) |