4HHE

Quinolinate synthase from Pyrococcus furiosus

「2QS0」から置き換えられました

4HHE の概要

• エントリーDOI: 10.2210/pdb4hhe/pdb
• 分子名称: Quinolinate synthase A, CHLORIDE ION (2 entities in total)
• 機能のキーワード: quinolinate synthase, nad biosynthesis, nada, pyridine nucleotide biosynthesis, biosynthetic protein, transferase
• 由来する生物種: Pyrococcus furiosus
• 細胞内の位置: Cytoplasm (By similarity): Q8TZL3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36702.47

構造登録者

Soriano, E.V.,Zhang, Y.,Settembre, E.C.,Colabroy, K.,Sanders, J.M.,Dorrestein, P.C.,Begley, T.P.,Ealick, S.E. (登録日: 2012-10-09, 公開日: 2013-08-28, 最終更新日: 2024-02-28)

主引用文献

Soriano, E.V.,Zhang, Y.,Colabroy, K.L.,Sanders, J.M.,Settembre, E.C.,Dorrestein, P.C.,Begley, T.P.,Ealick, S.E.
Active-site models for complexes of quinolinate synthase with substrates and intermediates.
Acta Crystallogr.,Sect.D, 69:1685-1696, 2013

PubMed Abstract: Quinolinate synthase (QS) catalyzes the condensation of iminoaspartate and dihydroxyacetone phosphate to form quinolinate, the universal precursor for the de novo biosynthesis of nicotinamide adenine dinucleotide. QS has been difficult to characterize owing either to instability or lack of activity when it is overexpressed and purified. Here, the structure of QS from Pyrococcus furiosus has been determined at 2.8 Å resolution. The structure is a homodimer consisting of three domains per protomer. Each domain shows the same topology with a four-stranded parallel β-sheet flanked by four α-helices, suggesting that the domains are the result of gene triplication. Biochemical studies of QS indicate that the enzyme requires a [4Fe-4S] cluster, which is lacking in this crystal structure, for full activity. The organization of domains in the protomer is distinctly different from that of a monomeric structure of QS from P. horikoshii [Sakuraba et al. (2005), J. Biol. Chem. 280, 26645-26648]. The domain arrangement in P. furiosus QS may be related to protection of cysteine side chains, which are required to chelate the [4Fe-4S] cluster, prior to cluster assembly.

PubMed: 23999292
DOI: 10.1107/S090744491301247X

実験手法

X-RAY DIFFRACTION (2.797 Å)