1lld

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[[Image:1lld.gif|left|200px]]
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{{Seed}}
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[[Image:1lld.png|left|200px]]
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{{STRUCTURE_1lld| PDB=1lld | SCENE= }}
{{STRUCTURE_1lld| PDB=1lld | SCENE= }}
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'''MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE'''
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===MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8450537 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8450537}}
==About this Structure==
==About this Structure==
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[[Category: Iwata, S.]]
[[Category: Iwata, S.]]
[[Category: Ohta, T.]]
[[Category: Ohta, T.]]
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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 Wed Jul 2 21:22:34 2008''

Revision as of 18:22, 2 July 2008

Image:1lld.png

Template:STRUCTURE 1lld

MOLECULAR BASIS OF ALLOSTERIC ACTIVATION OF BACTERIAL L-LACTATE DEHYDROGENASE

Template:ABSTRACT PUBMED 8450537

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 Wed Jul 2 21:22:34 2008

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