Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism

l-2-Keto-3-deoxyarabonate (l-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of l-KDA to α-ketoglutaric semialdehyde. l-KDA dehydratase was overexpressed, purified and crystallized at 291 K usin...

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Detalles Bibliográficos
Autores principales: Shimada, Naoko, Mikami, Bunzo, Watanabe, Seiya, Makino, Keisuke
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2007
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2334997/
https://www.ncbi.nlm.nih.gov/pubmed/17565178
http://dx.doi.org/10.1107/S1744309107015102
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author Shimada, Naoko
Mikami, Bunzo
Watanabe, Seiya
Makino, Keisuke
author_facet Shimada, Naoko
Mikami, Bunzo
Watanabe, Seiya
Makino, Keisuke
author_sort Shimada, Naoko
collection PubMed
description l-2-Keto-3-deoxyarabonate (l-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of l-KDA to α-ketoglutaric semialdehyde. l-KDA dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 Å resolution using synchrotron radiation and belongs to the trigonal space group P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 78.91, c = 207.71 Å.
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spelling pubmed-23349972008-05-12 Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism Shimada, Naoko Mikami, Bunzo Watanabe, Seiya Makino, Keisuke Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications l-2-Keto-3-deoxyarabonate (l-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of l-KDA to α-ketoglutaric semialdehyde. l-KDA dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 Å resolution using synchrotron radiation and belongs to the trigonal space group P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 78.91, c = 207.71 Å. International Union of Crystallography 2007-04-06 /pmc/articles/PMC2334997/ /pubmed/17565178 http://dx.doi.org/10.1107/S1744309107015102 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
Shimada, Naoko
Mikami, Bunzo
Watanabe, Seiya
Makino, Keisuke
Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title_full Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title_fullStr Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title_full_unstemmed Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title_short Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
title_sort preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2334997/
https://www.ncbi.nlm.nih.gov/pubmed/17565178
http://dx.doi.org/10.1107/S1744309107015102
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AT mikamibunzo preliminarycrystallographicanalysisofl2keto3deoxyarabonatedehydrataseanenzymeinvolvedinanalternativebacterialpathwayoflarabinosemetabolism
AT watanabeseiya preliminarycrystallographicanalysisofl2keto3deoxyarabonatedehydrataseanenzymeinvolvedinanalternativebacterialpathwayoflarabinosemetabolism
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