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Structural insights into the bacterial carbon-phosphorus lyase machinery

Phosphorous 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 organic phosphonate compounds, which require specialised enzymatic machinery for breaking the stable ca...

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Autores principales: Seweryn, Paulina, Van, Lan Bich, Kjeldgaard, Morten, Russo, Christopher J., Passmore, Lori A., Hove-Jensen, Bjarne, Jochimsen, Bjarne, Brodersen, Ditlev E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4617613/
https://www.ncbi.nlm.nih.gov/pubmed/26280334
http://dx.doi.org/10.1038/nature14683
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author Seweryn, Paulina
Van, Lan Bich
Kjeldgaard, Morten
Russo, Christopher J.
Passmore, Lori A.
Hove-Jensen, Bjarne
Jochimsen, Bjarne
Brodersen, Ditlev E.
author_facet Seweryn, Paulina
Van, Lan Bich
Kjeldgaard, Morten
Russo, Christopher J.
Passmore, Lori A.
Hove-Jensen, Bjarne
Jochimsen, Bjarne
Brodersen, Ditlev E.
author_sort Seweryn, Paulina
collection PubMed
description Phosphorous 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 organic phosphonate compounds, which require specialised enzymatic machinery for breaking the stable carbon-phosphorus (C-P) bond. Despite its importance, the details of how this machinery catabolises phosphonate remain unknown. Here we determine the crystal structure of the 240 kDa Escherichia coli C-P lyase core complex (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 likely couple organic 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 PhnJ via a conserved insertion domain. Our results provide a structural basis for understanding microbial phosphonate breakdown.
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spelling pubmed-46176132016-03-03 Structural insights into the bacterial carbon-phosphorus lyase machinery Seweryn, Paulina Van, Lan Bich Kjeldgaard, Morten Russo, Christopher J. Passmore, Lori A. Hove-Jensen, Bjarne Jochimsen, Bjarne Brodersen, Ditlev E. Nature Article Phosphorous 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 organic phosphonate compounds, which require specialised enzymatic machinery for breaking the stable carbon-phosphorus (C-P) bond. Despite its importance, the details of how this machinery catabolises phosphonate remain unknown. Here we determine the crystal structure of the 240 kDa Escherichia coli C-P lyase core complex (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 likely couple organic 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 PhnJ via a conserved insertion domain. Our results provide a structural basis for understanding microbial phosphonate breakdown. 2015-08-17 2015-09-03 /pmc/articles/PMC4617613/ /pubmed/26280334 http://dx.doi.org/10.1038/nature14683 Text en Reprints and permissions information is available at www.nature.com/reprints (http://www.nature.com/reprints) Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Seweryn, Paulina
Van, Lan Bich
Kjeldgaard, Morten
Russo, Christopher J.
Passmore, Lori A.
Hove-Jensen, Bjarne
Jochimsen, Bjarne
Brodersen, Ditlev E.
Structural insights into the bacterial carbon-phosphorus lyase machinery
title Structural insights into the bacterial carbon-phosphorus lyase machinery
title_full Structural insights into the bacterial carbon-phosphorus lyase machinery
title_fullStr Structural insights into the bacterial carbon-phosphorus lyase machinery
title_full_unstemmed Structural insights into the bacterial carbon-phosphorus lyase machinery
title_short Structural insights into the bacterial carbon-phosphorus lyase machinery
title_sort structural insights into the bacterial carbon-phosphorus lyase machinery
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4617613/
https://www.ncbi.nlm.nih.gov/pubmed/26280334
http://dx.doi.org/10.1038/nature14683
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