1LLD

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Summary for 1LLD

• Entry DOI: 10.2210/pdb1lld/pdb
• Descriptor: L-LACTATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(choh (d)-nad (a)), oxidoreductase
• Biological source: Bifidobacterium longum subsp. longum
• Total number of polymer chains: 2
• Total formula weight: 69584.40

Authors

Iwata, S.,Ohta, T. (deposition date: 1992-06-08, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Iwata, S.,Ohta, T.
Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
J.Mol.Biol., 230:21-27, 1993

PubMed Abstract: The three-dimensional structure of allosteric L-lactate dehydrogenase from Bifidobacterium longum, the first example of a T-state structure of L-lactate dehydrogenase, has been determined to 2.0 A. A comparative study of this structure with the previously reported R-state structure from Bacillus stearothermophilus has revealed the allosteric activation mechanism of the bacterial L-lactate dehydrogenase. The fructose 1,6-bisphosphate-induced conformational change at the effector site and the substrate affinity change at the activity site are clearly shown at a molecular level. Coupling of these changes can be simply explained by a set of concerted rotations between subunits in the tetramer of the enzyme. This T to R transition is the first example for a tetrameric allosteric protein where the rotations occur around each of three axes of symmetry.

PubMed: 8450537
DOI: 10.1006/jmbi.1993.1122

Experimental method

X-RAY DIFFRACTION (2 Å)