1lld: Difference between revisions

Revision as of 21:22, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lld.png

Template:STRUCTURE 1lld

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASEMOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Template:ABSTRACT PUBMED 8450537

About this StructureAbout this Structure

1LLD is a Single protein structure of sequence from Bifidobacterium longum bv. longum. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase., Iwata S, Ohta T, J Mol Biol. 1993 Mar 5;230(1):21-7. PMID:8450537

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-'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''
+===MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8450537}}, adds the Publication Abstract to the page
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