We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1lth

From Proteopedia

Revision as of 11:48, 21 February 2008 by OCA (Talk | contribs)
Jump to: navigation, search
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

Page seeded by OCA on Thu Feb 21 13:48:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lth"
Personal tools