1lld: Difference between revisions
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==MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE== | ==MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE== | ||
<StructureSection load='1lld' size='340' side='right' caption='[[1lld]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1lld' size='340' side='right'caption='[[1lld]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lld]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_biovar_longum Bifidobacterium longum biovar longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LLD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1lld]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_biovar_longum Bifidobacterium longum biovar longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LLD FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1lld_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1lld_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1lld" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1lld" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bifidobacterium longum biovar longum]] | [[Category: Bifidobacterium longum biovar longum]] | ||
[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Iwata, S]] | [[Category: Iwata, S]] | ||
[[Category: Ohta, T]] | [[Category: Ohta, T]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 15:06, 13 November 2019
MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASEMOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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