Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery

Publikation: KonferencebidragPosterForskningpeer review

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Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. / Brodersen, Ditlev Egeskov.

2015. Poster session præsenteret ved Gordon Research Conference, Waterville Valley, NH, USA.

Publikation: KonferencebidragPosterForskningpeer review

Harvard

Brodersen, DE 2015, 'Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery', Gordon Research Conference, Waterville Valley, NH, USA, 12/07/2015 - 17/07/2015.

APA

Brodersen, D. E. (2015). Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. Poster session præsenteret ved Gordon Research Conference, Waterville Valley, NH, USA.

CBE

Brodersen DE. 2015. Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. Poster session præsenteret ved Gordon Research Conference, Waterville Valley, NH, USA.

MLA

Brodersen, Ditlev Egeskov Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. Gordon Research Conference, 12 jul. 2015, Waterville Valley, NH, USA, Poster, 2015. 1 s.

Vancouver

Brodersen DE. Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. 2015. Poster session præsenteret ved Gordon Research Conference, Waterville Valley, NH, USA.

Author

Brodersen, Ditlev Egeskov. / Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery. Poster session præsenteret ved Gordon Research Conference, Waterville Valley, NH, USA.1 s.

Bibtex

@conference{d5ce9c5b550f469a9ddb89b00bec6cdb,
title = "Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery",
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 {\AA} 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.",
author = "Brodersen, {Ditlev Egeskov}",
year = "2015",
month = "7",
day = "12",
language = "English",
note = "Gordon Research Conference : Enzymes, Coenzymes & Metabolic Pathways ; Conference date: 12-07-2015 Through 17-07-2015",

}

RIS

TY - CONF

T1 - Structural Insights Into The Bacterial Carbon-Phosphorus Lyase Machinery

AU - Brodersen, Ditlev Egeskov

PY - 2015/7/12

Y1 - 2015/7/12

N2 - 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.

AB - 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.

M3 - Poster

ER -