1WZU

Crystal structure of quinolinate synthase (nadA)

Summary for 1WZU

• Entry DOI: 10.2210/pdb1wzu/pdb
• Descriptor: Quinolinate synthetase A, D-MALATE (3 entities in total)
• Functional Keywords: nad, biosynthetic protein
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm (By similarity): O57767
• Total number of polymer chains: 1
• Total formula weight: 34324.11

Authors

Sakuraba, H. (deposition date: 2005-03-09, release date: 2005-06-07, Last modification date: 2024-03-13)

Primary citation

Sakuraba, H.,Tsuge, H.,Yoneda, K.,Katunuma, N.,Ohshima, T.
Crystal Structure of the NAD Biosynthetic Enzyme Quinolinate Synthase
J.Biol.Chem., 280:26645-26648, 2005

PubMed Abstract: A gene encoding a quinolinate synthase has been identified in the hyperthermophilic archaeon Pyrococcus horikoshii via genome sequencing. The gene was overexpressed in Escherichia coli, and the crystal structure of the produced enzyme was determined to 2.0 A resolution in the presence of malate, a substrate analogue. The overall structure exhibits a unique triangular architecture composed of a 3-fold repeat of three-layer (alphabetaalpha) sandwich folding. Although some aspects of the fold homologous to the each domain have been observed previously, the overall structure of quinolinate synthase shows no similarity to any known protein structure. The three analogous domains are related to a pseudo-3-fold symmetry. The active site is located at the interface of the three domains and is centered on the pseudo-3-fold axis. The malate molecule is tightly held near the bottom of the active site cavity. The model of the catalytic state during the first condensation step of the quinolinate synthase reaction indicates that the elimination of inorganic phosphate from dihydroxyacetone phosphate may precede the condensation reaction.

PubMed: 15937336
DOI: 10.1074/jbc.C500192200

Experimental method

X-RAY DIFFRACTION (2 Å)