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1sg6
From Proteopedia
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | AROMA, AROM (Emericella nidulans) | ||||||
| Activity: | 3-dehydroquinate synthase, with EC number 4.2.3.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 14:04:30 2008
