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Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 Å resolution from crystals grown following enzyme turnover

Lookup NU author(s): Professor Alastair Hawkins

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Abstract

Crystallization of Aspergillus nidulans 3-dehydroquinate synthase (DHQS), following turnover of the enzyme by addition of the substrate DAHP, gave ä new crystal form (form J). Although the crystals have dimensions of only 50 × 20 × 5 μm, they are well ordered, diffracting to 1.7 Å. The space group is C2221, with unit-cell parameters a = 90.0, b = 103.7, c = 177.4 Å. Structure determination and refinement to R = 0.19 (Rfree = 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 Å resolution. The use of enzyme turnover may be applicable in other systems in attempts to improve crystal quality. © 2004 International Union of Crystallography. Printed in Denmark - all rights reserved.

Publication metadata

Author(s): Nichols CE, Hawkins AR, Stammers DK

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica Section D: Biological Crystallography

Year: 2004

Volume: 60

Issue: 5

Pages: 971-973

ISSN (print): 0907-4449

ISSN (electronic): 1399-0047

Publisher: Wiley-Blackwell

URL: http://dx.doi.org/10.1107/S0907444904004743

DOI: 10.1107/S0907444904004743

PubMed id: 15103156

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