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Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
1,3-Propanediol dehydrogenase (1,3-PD-DH), encoded by the dhaT gene, is a key enzyme in the dissimilation process for converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae. Single colourless crystals were obtained from a recombinant preparation of 1,3-propanediol dehydro...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330189/ https://www.ncbi.nlm.nih.gov/pubmed/17329826 http://dx.doi.org/10.1107/S1744309107008834 |
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author | Marçal, D. Rego, A. T. Fogg, M. J. Wilson, K. S. Carrondo, M. A. Enguita, F. J. |
author_facet | Marçal, D. Rego, A. T. Fogg, M. J. Wilson, K. S. Carrondo, M. A. Enguita, F. J. |
author_sort | Marçal, D. |
collection | PubMed |
description | 1,3-Propanediol dehydrogenase (1,3-PD-DH), encoded by the dhaT gene, is a key enzyme in the dissimilation process for converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae. Single colourless crystals were obtained from a recombinant preparation of 1,3-propanediol dehydrogenase overexpressed in Escherichia coli. The crystals belong to space group P2(1), with unit-cell parameters a = 91.9, b = 226.6, c = 232.6 Å, β = 92.9°. The crystals probably contain two decamers in the asymmetric unit, with a V (M) value of 3.07 Å(3) Da(−1) and an estimated solvent content of 59%. Diffraction data were collected to 2.7 Å resolution using synchrotron radiation at the ID14-4 beamline of the European Synchrotron Radiation Facility. |
format | Text |
id | pubmed-2330189 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-23301892008-05-12 Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae Marçal, D. Rego, A. T. Fogg, M. J. Wilson, K. S. Carrondo, M. A. Enguita, F. J. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications 1,3-Propanediol dehydrogenase (1,3-PD-DH), encoded by the dhaT gene, is a key enzyme in the dissimilation process for converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae. Single colourless crystals were obtained from a recombinant preparation of 1,3-propanediol dehydrogenase overexpressed in Escherichia coli. The crystals belong to space group P2(1), with unit-cell parameters a = 91.9, b = 226.6, c = 232.6 Å, β = 92.9°. The crystals probably contain two decamers in the asymmetric unit, with a V (M) value of 3.07 Å(3) Da(−1) and an estimated solvent content of 59%. Diffraction data were collected to 2.7 Å resolution using synchrotron radiation at the ID14-4 beamline of the European Synchrotron Radiation Facility. International Union of Crystallography 2007-02-28 /pmc/articles/PMC2330189/ /pubmed/17329826 http://dx.doi.org/10.1107/S1744309107008834 Text en © International Union of Crystallography 2007 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Crystallization Communications Marçal, D. Rego, A. T. Fogg, M. J. Wilson, K. S. Carrondo, M. A. Enguita, F. J. Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae |
title | Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
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title_full | Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
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title_fullStr | Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
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title_full_unstemmed | Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
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title_short | Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae
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title_sort | crystallization and preliminary x-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen klebsiella pneumoniae |
topic | Crystallization Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330189/ https://www.ncbi.nlm.nih.gov/pubmed/17329826 http://dx.doi.org/10.1107/S1744309107008834 |
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