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-Structure paper
タイトル | Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 1001, Year 2023 |
掲載日 | 2023年2月22日 |
著者 | Søren K Amstrup / Sui Ching Ong / Nicholas Sofos / Jesper L Karlsen / Ragnhild B Skjerning / Thomas Boesen / Jan J Enghild / Bjarne Hove-Jensen / Ditlev E Brodersen / |
PubMed 要旨 | In Escherichia coli, the 14-cistron phn operon encoding carbon-phosphorus lyase allows for utilisation of phosphorus from a wide range of stable phosphonate compounds containing a C-P bond. As part ...In Escherichia coli, the 14-cistron phn operon encoding carbon-phosphorus lyase allows for utilisation of phosphorus from a wide range of stable phosphonate compounds containing a C-P bond. As part of a complex, multi-step pathway, the PhnJ subunit was shown to cleave the C-P bond via a radical mechanism, however, the details of the reaction could not immediately be reconciled with the crystal structure of a 220 kDa PhnGHIJ C-P lyase core complex, leaving a significant gap in our understanding of phosphonate breakdown in bacteria. Here, we show using single-particle cryogenic electron microscopy that PhnJ mediates binding of a double dimer of the ATP-binding cassette proteins, PhnK and PhnL, to the core complex. ATP hydrolysis induces drastic structural remodelling leading to opening of the core complex and reconfiguration of a metal-binding and putative active site located at the interface between the PhnI and PhnJ subunits. |
リンク | Nat Commun / PubMed:36813778 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 1.93 - 2.57 Å |
構造データ | EMDB-14441, PDB-7z15: EMDB-14442, PDB-7z16: EMDB-14443, PDB-7z17: EMDB-14444, PDB-7z18: EMDB-14445, PDB-7z19: |
化合物 | ChemComp-ZN: ChemComp-I9X: ChemComp-ADP: ChemComp-PO4: ChemComp-MG: ChemComp-ATP: ChemComp-HOH: ChemComp-ANP: |
由来 |
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キーワード | TRANSFERASE / protein complex / ABC / hydrolase / lyase / carbon phosphorus / carbon-phosphorus / SAM |