1lld
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(New page: 200px<br /><applet load="1lld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lld, resolution 2.0Å" /> '''MOLECULAR BASIS OF AL...)
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Revision as of 18:31, 20 November 2007
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MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE
Overview
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.
About this Structure
1LLD is a Single protein structure of sequence from Bifidobacterium longum bv. longum with NAD as ligand. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
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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