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|1sg6, resolution 1.70Å ()|
|Sites:||, , and|
|Gene:||AROMA, AROM (Emericella nidulans)|
|Related:||1nrx, 1nve, 1nvd, 1nvb, 1nua, 1nva, 1nvf, 1nr5|
Crystal structure of Aspergillus nidulans 3-dehydroquinate synthase (AnDHQS) in complex with Zn2+ and NAD+, at 1.7D
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Nichols CE, Hawkins AR, Stammers DK. Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover. Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):971-3. Epub 2004, Apr 21. PMID:15103156 doi:10.1107/S0907444904004743