1SG6

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

Summary for 1SG6

• Entry DOI: 10.2210/pdb1sg6/pdb
• Related: 1NR5 1NRX 1NUA 1NVA 1NVB 1NVD 1NVE 1NVF
• Descriptor: Pentafunctional AROM polypeptide, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: shikimate pathway, aromatic amino acid biosynthesis, dhqs, open form, form j, domain movement, cyclase, lyase
• Biological source: Emericella nidulans
• Cellular location: Cytoplasm: P07547
• Total number of polymer chains: 2
• Total formula weight: 87390.74

Authors

Nichols, C.E.,Hawkins, A.R.,Stammers, D.K. (deposition date: 2004-02-23, release date: 2004-08-31, Last modification date: 2023-08-23)

Primary citation

Nichols, C.E.,Hawkins, A.R.,Stammers, D.K.
Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover.
Acta Crystallogr.,Sect.D, 60:971-973, 2004

PubMed Abstract: 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.

PubMed: 15103156
DOI: 10.1107/S0907444904004743

Experimental method

X-RAY DIFFRACTION (1.7 Å)