1lld: Difference between revisions
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[[Image:1lld.gif|left|200px]] | [[Image:1lld.gif|left|200px]] | ||
'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE''' | {{Structure | ||
|PDB= 1lld |SIZE=350|CAPTION= <scene name='initialview01'>1lld</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] | |||
|GENE= | |||
}} | |||
'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LLD is a [ | 1LLD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8450537 8450537] | ||
[[Category: Bifidobacterium longum bv. longum]] | [[Category: Bifidobacterium longum bv. longum]] | ||
[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
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[[Category: oxidoreductase(choh (d)-nad (a))]] | [[Category: oxidoreductase(choh (d)-nad (a))]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:17 2008'' | ||
Revision as of 10:32, 20 March 2008
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| 1lld, resolution 2.0Å | |||||||||||||
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| Ligands: | NAD | ||||||||||||
| Activity: | L-lactate dehydrogenase, with EC number 1.1.1.27 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:32:17 2008
