Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens

Helena Taberman; Martina Andberg; Tarja Parkkinen; Peter Richard; Nina Hakulinen; Anu Koivula; Juha Rouvinen

doi:10.1107/S2053230X13031361

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens

Helena Taberman, Martina Andberg, Tarja Parkkinen, Peter Richard, Nina Hakulinen, Anu Koivula, Juha Rouvinen (Corresponding Author)

University of Eastern Finland

Research output: Contribution to journal › Article › Scientific › peer-review

5 Citations (Scopus)

Abstract

D-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-D-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of D-galacturonic acid in Agrobacterium tumefaciens (At). It converts 3-deoxy-2-keto-L-threo-hexarate to α-ketoglutaric semialdehyde. At KDG dehydratase was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 169.1, b = 117.8, c = 74.3 Å, β = 112.4° and an asymmetric unit of four monomers. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The three-dimensional structure of At KDG dehydratase will provide valuable information on the function of the enzyme and will allow it to be engineered for biorefinery-based applications.

Original language	English
Pages (from-to)	49-52
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	70
DOIs	https://doi.org/10.1107/S2053230X13031361
Publication status	Published - 2014
MoE publication type	A1 Journal article-refereed

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10.1107/S2053230X13031361

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Taberman, H., Andberg, M., Parkkinen, T., Richard, P., Hakulinen, N., Koivula, A., & Rouvinen, J. (2014). Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens. Acta Crystallographica Section F: Structural Biology Communications, 70, 49-52. https://doi.org/10.1107/S2053230X13031361

@article{cab6903cd478427bb46dca949289cc6d,

title = "Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens",

abstract = "D-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-D-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of D-galacturonic acid in Agrobacterium tumefaciens (At). It converts 3-deoxy-2-keto-L-threo-hexarate to α-ketoglutaric semialdehyde. At KDG dehydratase was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 169.1, b = 117.8, c = 74.3 {\AA}, β = 112.4° and an asymmetric unit of four monomers. X-ray diffraction data were collected to 1.9 {\AA} resolution using synchrotron radiation. The three-dimensional structure of At KDG dehydratase will provide valuable information on the function of the enzyme and will allow it to be engineered for biorefinery-based applications.",

author = "Helena Taberman and Martina Andberg and Tarja Parkkinen and Peter Richard and Nina Hakulinen and Anu Koivula and Juha Rouvinen",

year = "2014",

doi = "10.1107/S2053230X13031361",

language = "English",

volume = "70",

pages = "49--52",

journal = "Acta Crystallographica Section F: Structural Biology Communications",

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publisher = "International Union of Crystallography",

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Taberman, H, Andberg, M, Parkkinen, T, Richard, P, Hakulinen, N, Koivula, A & Rouvinen, J 2014, 'Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens', Acta Crystallographica Section F: Structural Biology Communications, vol. 70, pp. 49-52. https://doi.org/10.1107/S2053230X13031361

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens. / Taberman, Helena; Andberg, Martina; Parkkinen, Tarja et al.
In: Acta Crystallographica Section F: Structural Biology Communications, Vol. 70, 2014, p. 49-52.

Research output: Contribution to journal › Article › Scientific › peer-review

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens

AU - Taberman, Helena

AU - Andberg, Martina

AU - Parkkinen, Tarja

AU - Richard, Peter

AU - Hakulinen, Nina

AU - Koivula, Anu

AU - Rouvinen, Juha

PY - 2014

Y1 - 2014

N2 - D-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-D-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of D-galacturonic acid in Agrobacterium tumefaciens (At). It converts 3-deoxy-2-keto-L-threo-hexarate to α-ketoglutaric semialdehyde. At KDG dehydratase was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 169.1, b = 117.8, c = 74.3 Å, β = 112.4° and an asymmetric unit of four monomers. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The three-dimensional structure of At KDG dehydratase will provide valuable information on the function of the enzyme and will allow it to be engineered for biorefinery-based applications.

AB - D-Galacturonic acid is the main component of pectin. It could be used to produce affordable renewable fuels, chemicals and materials through biotechnical conversion. Keto-deoxy-D-galactarate (KDG) dehydratase is an enzyme in the oxidative pathway of D-galacturonic acid in Agrobacterium tumefaciens (At). It converts 3-deoxy-2-keto-L-threo-hexarate to α-ketoglutaric semialdehyde. At KDG dehydratase was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 169.1, b = 117.8, c = 74.3 Å, β = 112.4° and an asymmetric unit of four monomers. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The three-dimensional structure of At KDG dehydratase will provide valuable information on the function of the enzyme and will allow it to be engineered for biorefinery-based applications.

U2 - 10.1107/S2053230X13031361

DO - 10.1107/S2053230X13031361

M3 - Article

SN - 2053-230X

VL - 70

SP - 49

EP - 52

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

ER -

Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-D-galactarate (KDG) dehydratase from Agrobacterium tumefaciens

Abstract

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