1saz

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spinqualitylabelsall models 1saz, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Membership in the ASKHA Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 from Thermotoga maritima

Overview

The sitting-drop method of crystallization uses the evaporation of water, to increase the concentration of the protein and precipitant in the drop., The presence of other volatile components, such as acetic acid, can have a, marked impact on crystallization. A member of the ASKHA (acetate and sugar, kinases/Hsc70/actin) superfamily of proteins, isobutyrate kinase (Buk2), from Thermotoga maritima, was expressed in Escherichia coli with six, histidine residues added to the C-terminus. The purified protein was, crystallized in a sitting drop with a well solution consisting of 1.7-3.0, M sodium formate, with the pH of the well solution alone adjusted to 4.5, with acetic acid. Diffraction data collected at 100 K show that the, crystals diffract to 3.1 A and belong to space group I422, with unit-cell, parameters a = b = 198.12, c = 58.93 A. Both the crystal form and the, results of dynamic light-scattering studies suggest that Buk2 is an, octomer, the first to be identified in the ASKHA superfamily.

About this Structure

1SAZ is a Single protein structure of sequence from Thermotoga maritima with NA, ACP and FMT as ligands. Active as Butyrate kinase, with EC number 2.7.2.7 Full crystallographic information is available from OCA.

Reference

Crystallization of butyrate kinase 2 from Thermotoga maritima mediated by vapor diffusion of acetic acid., Diao J, Cooper DR, Sanders DA, Hasson MS, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1100-2. Epub 2003, May 23. PMID:12777787

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