Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus.
The D-lactate dehydrogenase (D-LDH) from Lactobacillus bulgaricus has been purified and co-crystallized with its cofactor NAD+. Crystals suitable for X-ray diffraction experiments have been obtained from an ammonium sulfate solution by the hanging-drop method. The crystals belong to the orthorhombic space group C222 (or C222(1)) with cell dimensions a = 76.5 A, b = 93.3 A, c = 118.4 A and one monomer of 37,000 daltons per asymmetric unit. They diffract beyond 3.0 A resolution. Sequence comparison suggests that D-LDHs have no evolutionary relationship to L-LDHs and belong instead to the family of the D-2-hydroxyacid dehydrogenases. The X-ray crystallographic structure of the D-LDH from Lactobacillus bulgaricus will be a decisive test of this hypothesis.
Nessler
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S
Laboratoire de Biologie Structurale, UMR 9920 CNRS-Université Paris-Sud, Orsay, France.
Le Bras
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G
Le Bras
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Garel
J R
JR
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D007770:L-Lactate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D007778:Lactobacillus / Q000201:enzymology*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D007770:L-Lactate Dehydrogenase