1LTH

T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

Summary for 1LTH

• Entry DOI: 10.2210/pdb1lth/pdb
• Descriptor: L-LACTATE DEHYDROGENASE (T- AND R- STATE TETRAMER COMPLEX), 1,6-di-O-phosphono-beta-D-fructofuranose, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: oxidoreductase, choh(d)-nad(a), allosteric enzyme
• Biological source: Bifidobacterium longum subsp. longum
• Cellular location: Cytoplasm: P19869
• Total number of polymer chains: 2
• Total formula weight: 70353.69

Authors

Iwata, S.,Ohta, T. (deposition date: 1995-01-04, release date: 1995-03-31, Last modification date: 2024-02-14)

Primary citation

Iwata, S.,Kamata, K.,Yoshida, S.,Minowa, T.,Ohta, T.
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
Nat.Struct.Biol., 1:176-185, 1994

PubMed Abstract: The crystal structure of L-lactate dehydrogenase from Bifidobacterium longum, determined to 2.5 A resolution, contains a regular 1:1 complex of T- and R-state tetramers. A comparison of these two structures within the same crystal lattice and kinetical characterization of the T-R transition in solution provide an explanation for the molecular mechanism of allosteric activation. Substrate affinity is controlled by helix sliding between subunits which is triggered by the binding of the activator, fructose 1,6-bisphosphate. The proposed mechanism can explain activation by chemical modification and mutagenesis, as well as suggesting why vertebrate counterparts are not allosteric.

PubMed: 7656036
DOI: 10.1038/nsb0394-176

Experimental method

X-RAY DIFFRACTION (2.5 Å)