2j0x

From Proteopedia

Revision as of 09:50, 30 October 2007

CRYSTAL STRUCTURE OF E. COLI ASPARTOKINASE III IN COMPLEX WITH LYSINE AND ASPARTATE (T-STATE)

Overview

Aspartokinase III (AKIII) from Escherichia coli catalyzes an initial, commitment step of the aspartate pathway, giving biosynthesis of certain, amino acids including lysine. We report crystal structures of AKIII in the, inactive T-state with bound feedback allosteric inhibitor lysine and in, the R-state with aspartate and ADP. The structures reveal an unusual, configuration for the regulatory ACT domains, in which ACT2 is inserted, into ACT1 rather than the expected tandem repeat. Comparison of R- and, T-state AKIII indicates that binding of lysine to the regulatory ACT1, domain in R-state AKIII instigates a series of changes that release a, "latch", the beta15-alphaK loop, from the catalytic domain, which in turn, undergoes large rotational rearrangements, promoting tetramer formation, ... [(full description)]

About this Structure

2J0X is a [Single protein] structure of sequence from [Escherichia coli] with PO4, ASP and LYS as [ligands]. Active as [Aspartate kinase], with EC number [2.7.2.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine., Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK, J Biol Chem. 2006 Oct 20;281(42):31544-52. Epub 2006 Aug 12. PMID:16905770

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