1LTH image
Deposition Date 1995-01-04
Release Date 1995-03-31
Last Version Date 2024-02-14
Entry Detail
PDB ID:
1LTH
Keywords:
OXIDOREDUCTASE
Title:
T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL
Biological Source:
Source Organism(s):
Bifidobacterium longum subsp. longum (Taxon ID: 1679)
Expression System(s):
Escherichia coli
Method Details:
Experimental Method:
X-RAY DIFFRACTION
Resolution:
2.50 Å
R-Value Work:
0.18
R-Value Observed:
0.18
Space Group:
F 2 2 2
1LTH validation report missing
Macromolecular Entities
Structures with similar UniProt ID
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:L-LACTATE DEHYDROGENASE (T- A
Chain IDs:A (auth: T), B (auth: R)
Chain Length:319
Number of Molecules:2
Biological Source:Bifidobacterium longum subsp. longum
UniProt ID:E8ME30 Pfam ID:PF00056, PF02866 EC:1.1.1.27
Ligand Molecules
FBP
NAD
OXM
Primary Citation
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)
PMID: 7656036 DOI: 10.1038/nsb0394-176

Abstact

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.

Legend

Protein

Chemical

Disease

Primary Citation of related structures
1LTH
Feedback Form
Name
Email
Institute
Feedback