1lth: Difference between revisions

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[[Image:1lth.~~jpg~~|left|200px]]

[[Image:1lth.png|left|200px]]

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~~==Overview==~~

The crystal structure of L-lactate dehydrogenase from Bifidobacterium longum, determined to 2.5 A resolution, contains a regular 1:1 complex of T- and R-state tetramers. A comparison of these two structures within the same crystal lattice and kinetical characterization of the T-R transition in solution provide an explanation for the molecular mechanism of allosteric activation. Substrate affinity is controlled by helix sliding between subunits which is triggered by the binding of the activator, fructose 1,6-bisphosphate. The proposed mechanism can explain activation by chemical modification and mutagenesis, as well as suggesting why vertebrate counterparts are not allosteric.

==About this Structure==

1LTH 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=1LTH OCA].

~~==Reference==~~

T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control., Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T, Nat Struct Biol. 1994 Mar;1(3):176-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7656036 7656036]

[[Category: Bifidobacterium longum bv. longum]]

[[Category: L-lactate dehydrogenase]]

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[[Category: Iwata, S.]]

[[Category: Ohta, T.]]

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-[[Image:1lth.jpg|left|200px]]
+[[Image:1lth.png|left|200px]]
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-==Overview==
+{{ABSTRACT_7656036}}
-The crystal structure of L-lactate dehydrogenase from Bifidobacterium longum, determined to 2.5 A resolution, contains a regular 1:1 complex of T- and R-state tetramers. A comparison of these two structures within the same crystal lattice and kinetical characterization of the T-R transition in solution provide an explanation for the molecular mechanism of allosteric activation. Substrate affinity is controlled by helix sliding between subunits which is triggered by the binding of the activator, fructose 1,6-bisphosphate. The proposed mechanism can explain activation by chemical modification and mutagenesis, as well as suggesting why vertebrate counterparts are not allosteric.
 ==About this Structure==
 LTH 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=1LTH OCA].
-==Reference==
-T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control., Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T, Nat Struct Biol. 1994 Mar;1(3):176-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7656036 7656036]
 [[Category: Bifidobacterium longum bv. longum]]
 [[Category: L-lactate dehydrogenase]]
@@ Line 25: / Line 21: @@
 [[Category: Iwata, S.]]
 [[Category: Ohta, T.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:16:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:41:26 2008''