A regular 1:1 complex of two allosteric states in the single crystal of L-lactate dehydrogenase from Bifidobacterium longum

J Mol Biol. 1994 Feb 25;236(3):958-9. doi: 10.1006/jmbi.1994.1202.

Abstract

Single crystals of the regular 1:1 complex of T and R-state tetramers of L-lactate dehydrogenase from Bifidobacterium longum have been grown from polyethylene glycol 6000 solution in the presence of NADH, fructose 1,6-bisphosphate and oxamate. The crystals belong to space group F222 with unit cell dimensions of a = 148.4 A, b = 295.9 A and c = 71.0 A. The crystals are suitable for X-ray analysis and diffract to beyond 2.5 A spacing. A crystallographic study showed that the asymmetric unit contains two subunits and that one of them belongs to the T-state tetramer and the other to the R-state tetramer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Site
  • Bifidobacterium / enzymology*
  • Crystallization
  • Crystallography, X-Ray / methods
  • L-Lactate Dehydrogenase / chemistry*
  • L-Lactate Dehydrogenase / isolation & purification
  • Macromolecular Substances
  • Models, Structural
  • Protein Conformation

Substances

  • Macromolecular Substances
  • L-Lactate Dehydrogenase