Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):124-6.

Crystallization of Arthrobacter sp. strain 1C N-(1-D-carboxyethyl)-L- norvaline dehydrogenase and its complex with NAD+.

Britton KL, Rogers HF, Asano Y, Dairi T, Kato Y, Stillman TJ.

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Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, England. k.britton@sheffield.ac.uk

Abstract

The novel NAD+-linked opine dehydrogenase from a soil isolate Arthrobacter sp. strain 1C belongs to an enzyme superfamily whose members exhibit quite diverse substrate specificities. Crystals of this opine dehydrogenase, obtained in the presence or absence of co-factor and substrates, have been shown to diffract to beyond 1.8 A resolution. X-ray precession photographs have established that the crystals belong to space group P21212, with cell parameters a = 104.9, b = 80.0, c = 45.5 A and a single subunit in the asymmetric unit. The elucidation of the three-dimensional structure of this enzyme will provide a structural framework for this novel class of dehydrogenases to enable a comparison to be made with other enzyme families and also as the basis for mutagenesis experiments directed towards the production of natural and synthetic opine-type compounds containing two chiral centres.

PMID:: 9867431; [PubMed - indexed for MEDLINE]

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Crystallization of Arthrobacter sp. strain 1C N-(1-D-carboxyethyl)-L-norvaline dehydrogenase and its complex with NAD+ [Acta Crystallogr D Biol Crysta...]
Crystallization of Arthrobacter sp. strain 1C N-(1-D-carboxyethyl)-L-norvaline dehydrogenase and its complex with NAD+
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Cited by 1 PubMed Central article

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Structures reported by this article

Crystal Structure Of The N-(1-D-Carboxylethyl)-L-Norvaline Dehydrogenase From Arthrobacter Sp. Strain 1c

PDB: 1BG6

Source: Arthrobacter sp. 1C

Method: X-Ray Diffraction

Resolution: 1.8 Å

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