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1lth

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(New page: 200px<br /><applet load="1lth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lth, resolution 2.5&Aring;" /> '''T AND R STATES IN THE...)
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[[Image:1lth.jpg|left|200px]]<br /><applet load="1lth" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1lth, resolution 2.5&Aring;" />
'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''<br />
'''T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1LTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum] with FBP, NAD and OXM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA].
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1LTH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_bv._longum Bifidobacterium longum bv. longum] with <scene name='pdbligand=FBP:'>FBP</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=OXM:'>OXM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTH OCA].
==Reference==
==Reference==
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[[Category: oxidoreductase (choh(d)-nad(a))]]
[[Category: oxidoreductase (choh(d)-nad(a))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:52:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:21 2008''

Revision as of 11:48, 21 February 2008

Image:1lth.jpg

1lth, resolution 2.5Å

Drag the structure with the mouse to rotate

T AND R STATES IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

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 Bifidobacterium longum bv. longum with , and as ligands. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from 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:7656036

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