1sg6

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Revision as of 00:14, 21 November 2007


1sg6, resolution 1.7Å

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Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D

Overview

Crystallization of Aspergillus nidulans 3-dehydroquinate synthase (DHQS), following turnover of the enzyme by addition of the substrate DAHP, gave a, new crystal form (form J). Although the crystals have dimensions of only, 50 x 20 x 5 micro m, they are well ordered, diffracting to 1.7 A. The, space group is C222(1), with unit-cell parameters a = 90.0, b = 103.7, c =, 177.4 A. Structure determination and refinement to R = 0.19 (R(free) =, 0.25) shows the DHQS is in the 'open' form with the substrate site, unoccupied but with some loop regions perturbed. Previous crystals of, open-form DHQS only diffracted to 2.5 A resolution. The use of enzyme, turnover may be applicable in other systems in attempts to improve crystal, quality.

About this Structure

1SG6 is a Single protein structure of sequence from Emericella nidulans with ZN and NAD as ligands. Active as 3-dehydroquinate synthase, with EC number 4.2.3.4 Full crystallographic information is available from OCA.

Reference

Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover., Nichols CE, Hawkins AR, Stammers DK, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:15103156

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