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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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Revision as of 18:44, 20 November 2007

Image:1lth.jpg

1lth, resolution 2.5Å

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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 FBP, NAD and OXM 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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