Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus

S Nessler; G Le Bras; G Le Bras; J R Garel

doi:10.1016/s0022-2836(05)80043-9

Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus

J Mol Biol. 1994 Jan 7;235(1):370-1. doi: 10.1016/s0022-2836(05)80043-9.

Authors

S Nessler¹, G Le Bras, G Le Bras, J R Garel

Affiliation

¹ Laboratoire de Biologie Structurale, UMR 9920 CNRS-Université Paris-Sud, Orsay, France.

PMID: 8289259
DOI: 10.1016/s0022-2836(05)80043-9

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray / methods
L-Lactate Dehydrogenase / chemistry*
L-Lactate Dehydrogenase / isolation & purification
Lactobacillus / enzymology*
Protein Conformation*
X-Ray Diffraction

Substances

L-Lactate Dehydrogenase