Crystallization and preliminary X-ray diffraction studies of 6-phosphogluconate dehydrogenase from Lactococcus lactis

Citation
E. Tetaud et al., Crystallization and preliminary X-ray diffraction studies of 6-phosphogluconate dehydrogenase from Lactococcus lactis, ACT CRYST D, 54, 1998, pp. 1422-1424
Citations number
16
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
54
Year of publication
1998
Part
6
Pages
1422 - 1424
Database
ISI
SICI code
0907-4449(19981101)54:S2<1422:CAPXDS>2.0.ZU;2-N
Abstract
6-Phosphogluconate dehydrogenase is one of the seven enzymes involved in th e pentose phosphate pathway. Crystals of a mammalian and a protozoan enzyme have been obtained previously and structures determined. It is reported he re that a bacterial fi-phosphogluconate dehydrogenase, from Lactococcus lac tis, has been purified and used in crystallization trials. Large prisms sui table for a detailed structural analysis have been obtained and characteriz ed as orthorhombic, space group F222, with a = 70.4, b = 105.7, c = 474.6 A ngstrom. Diffraction has been observed to 2.2 Angstrom resolution using syn chrotron radiation. Structural analysis, in combination with ongoing bioche mical characterization, will assist the elucidation of the structure-activi ty relationships of this enzyme.