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1lld

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[[Image:1lld.gif|left|200px]]
[[Image:1lld.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1lld |SIZE=350|CAPTION= <scene name='initialview01'>1lld</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1lld", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1lld| PDB=1lld | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lld OCA], [http://www.ebi.ac.uk/pdbsum/1lld PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lld RCSB]</span>
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}}
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'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''
'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''
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[[Category: Iwata, S.]]
[[Category: Iwata, S.]]
[[Category: Ohta, T.]]
[[Category: Ohta, T.]]
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[[Category: oxidoreductase(choh (d)-nad (a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:02:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:17 2008''
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Revision as of 21:02, 2 May 2008

Image:1lld.gif

Template:STRUCTURE 1lld

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 Sat May 3 00:02:09 2008

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