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Crystallization and preliminary x-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Crystallization and preliminary x-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
Crystallization and preliminary x-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
The enzyme L-threonine dehydrogenase catalyses the NAD(+)-dependent conversion of L-threonine to 2-amino-3-ketobutyrate, which is the first reaction of a two-step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of L-threonine dehydrogenase (Tk-TDH) from the hyperthermophilic organism Thermococcus kodakaraensis KOD1 is reported. This threonine dehydrogenase consists of 350 amino acids, with a molecular weight of 38 kDa, and was prepared using an Escherichia coli expression system. The purified native protein was crystallized using the hanging-drop vapour-diffusion method and crystals grew in the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 124.5, c = 271.1 A. Diffraction data were collected to 2.6 A resolution and preliminary analysis indicates that there are four molecules in the asymmetric unit of the crystal.
l-threonine dehydrogenase, thermophiles
1744-3091
828-830
Bowyer, A.
bfa8d898-7590-4536-a9ce-1a626a46b15c
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Wright, J.N.
e53ee4b9-10f5-4365-a9f2-5a7b0eacd86d
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Bashir, Q.
860d3441-1d7c-4635-88a0-6e9b26f63f2a
Rashid, N.
ca94ad4e-c02a-4662-84d2-c28a648793be
Jamil, F.
a3660507-e703-48a7-99d8-b4a101645e18
Akhtar, M.
a4174002-a6bd-4678-8e63-4cbe607a672d
Bowyer, A.
bfa8d898-7590-4536-a9ce-1a626a46b15c
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Wright, J.N.
e53ee4b9-10f5-4365-a9f2-5a7b0eacd86d
Coker, A.
c64a7d9b-3a0d-4e79-a3eb-aaa64920116a
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Bashir, Q.
860d3441-1d7c-4635-88a0-6e9b26f63f2a
Rashid, N.
ca94ad4e-c02a-4662-84d2-c28a648793be
Jamil, F.
a3660507-e703-48a7-99d8-b4a101645e18
Akhtar, M.
a4174002-a6bd-4678-8e63-4cbe607a672d

Bowyer, A., Mikolajek, H., Wright, J.N., Coker, A., Erskine, P.T., Cooper, J.B., Bashir, Q., Rashid, N., Jamil, F. and Akhtar, M. (2008) Crystallization and preliminary x-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis. Acta Crystallographica Section F: Structural Biology Communications, F64, part 9, 828-830. (doi:10.1107/S1744309108025384). (PMID:18765916)

Record type: Article

Abstract

The enzyme L-threonine dehydrogenase catalyses the NAD(+)-dependent conversion of L-threonine to 2-amino-3-ketobutyrate, which is the first reaction of a two-step biochemical pathway involved in the metabolism of threonine to glycine. Here, the crystallization and preliminary crystallographic analysis of L-threonine dehydrogenase (Tk-TDH) from the hyperthermophilic organism Thermococcus kodakaraensis KOD1 is reported. This threonine dehydrogenase consists of 350 amino acids, with a molecular weight of 38 kDa, and was prepared using an Escherichia coli expression system. The purified native protein was crystallized using the hanging-drop vapour-diffusion method and crystals grew in the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 124.5, c = 271.1 A. Diffraction data were collected to 2.6 A resolution and preliminary analysis indicates that there are four molecules in the asymmetric unit of the crystal.

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Published date: 20 August 2008
Keywords: l-threonine dehydrogenase, thermophiles
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 335748
URI: https://eprints.soton.ac.uk/id/eprint/335748
ISSN: 1744-3091
PURE UUID: a4ef0b27-a220-43fe-9e3e-d277f729684e
ORCID for H. Mikolajek: ORCID iD orcid.org/0000-0003-0776-9974

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Date deposited: 13 Mar 2012 13:28
Last modified: 18 Jul 2017 06:10

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