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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2015
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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. |
format | Online Article Text |
id | pubmed-4617613 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
record_format | MEDLINE/PubMed |
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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