2DC1

Crystal Structure Of L-Aspartate Dehydrogenase From Hyperthermophilic Archaeon Archaeoglobus fulgidus

Summary for 2DC1

• Entry DOI: 10.2210/pdb2dc1/pdb
• Descriptor: L-aspartate dehydrogenase, CITRIC ACID, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: l-aspartate dehydrogenase, nad, oxidoreductase
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 2
• Total formula weight: 54201.71

Authors

Yoneda, K.,Sakuraba, H.,Tsuge, H.,Ohshima, T. (deposition date: 2005-12-19, release date: 2006-12-26, Last modification date: 2024-03-13)

Primary citation

Yoneda, K.,Sakuraba, H.,Tsuge, H.,Katunuma, N.,Ohshima, T.
Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex.
Febs J., 274:4315-4325, 2007

PubMed Abstract: The crystal structure of the highly thermostable L-aspartate dehydrogenase (L-aspDH; EC 1.4.1.21) from the hyperthermophilic archaeon Archaeoglobus fulgidus was determined in the presence of NAD and a substrate analog, citrate. The dimeric structure of A. fulgidus L-aspDH was refined at a resolution of 1.9 A with a crystallographic R-factor of 21.7% (R(free) = 22.6%). The structure indicates that each subunit consists of two domains separated by a deep cleft containing an active site. Structural comparison of the A. fulgidus L-aspDH/NAD/citrate ternary complex and the Thermotoga maritima L-aspDH/NAD binary complex showed that A. fulgidus L-aspDH assumes a closed conformation and that a large movement of the two loops takes place during substrate binding. Like T. maritima L-aspDH, the A. fulgidus enzyme is highly thermostable. But whereas a large number of inter- and intrasubunit ion pairs are responsible for the stability of A. fulgidus L-aspDH, a large number of inter- and intrasubunit aromatic pairs stabilize the T. maritima enzyme. Thus stabilization of these two L-aspDHs appears to be achieved in different ways. This is the first detailed description of substrate and coenzyme binding to L-aspDH and of the molecular basis of the high thermostability of a hyperthermophilic L-aspDH.

PubMed: 17651440
DOI: 10.1111/j.1742-4658.2007.05961.x

Experimental method

X-RAY DIFFRACTION (1.9 Å)