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Crystallization and preliminary X-ray diffraction studies of 6-phosphogluconate dehydrogenase from Lactococcus lactis.
Tetaud, E; Hall, D R; Gourley, D G; Leonard, G A; Arkison, S; Barrett, M P; Hunter, W N.
Affiliation
  • Tetaud E; The Wellcome Trust Building, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland.
Acta Crystallogr D Biol Crystallogr ; 54(Pt 6 Pt 2): 1422-4, 1998 Nov 01.
Article in En | MEDLINE | ID: mdl-10089526
ABSTRACT
6-Phosphogluconate dehydrogenase is one of the seven enzymes involved in the pentose phosphate pathway. Crystals of a mammalian and a protozoan enzyme have been obtained previously and structures determined. It is reported here that a bacterial 6-phosphogluconate dehydrogenase, from Lactococcus lactis, has been purified and used in crystallization trials. Large prisms suitable for a detailed structural analysis have been obtained and characterized as orthorhombic, space group F222, with a = 70.4, b = 105.7, c = 474.6 A. Diffraction has been observed to 2.2 A resolution using synchrotron radiation. Structural analysis, in combination with ongoing biochemical characterization, will assist the elucidation of the structure-activity relationships of this enzyme.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Phosphogluconate Dehydrogenase / Bacterial Proteins / Lactococcus lactis Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 1998 Document type: Article Affiliation country: United kingdom
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Collection: 01-internacional Database: MEDLINE Main subject: Phosphogluconate Dehydrogenase / Bacterial Proteins / Lactococcus lactis Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 1998 Document type: Article Affiliation country: United kingdom