5DEL

Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM59

「4RYH」から置き換えられました

5DEL の概要

• エントリーDOI: 10.2210/pdb5del/pdb
• 分子名称: Dihydroorotate dehydrogenase (quinone), mitochondrial, FLAVIN MONONUCLEOTIDE, OROTIC ACID, ... (7 entities in total)
• 機能のキーワード: alpha/beta barrel, mitochondrial membrane, fmn, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor
• 由来する生物種: Plasmodium falciparum
• 細胞内の位置: Mitochondrion inner membrane ; Single-pass membrane protein : Q08210
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46737.09

構造登録者

Phillips, M.,Deng, X. (登録日: 2015-08-25, 公開日: 2015-10-07, 最終更新日: 2023-09-27)

主引用文献

Deng, X.,Matthews, D.,Rathod, P.K.,Phillips, M.A.
The X-ray structure of Plasmodium falciparum dihydroorotate dehydrogenase bound to a potent and selective N-phenylbenzamide inhibitor reveals novel binding-site interactions.
Acta Crystallogr.,Sect.F, 71:553-559, 2015

PubMed Abstract: Plasmodium species are protozoan parasites that are the causative agent of malaria. Malaria is a devastating disease, and its treatment and control have been hampered by the propensity of the parasite to become drug-resistant. Dihydroorotate dehydrogenase (DHODH) has been identified as a promising new target for the development of antimalarial agents. Here, the X-ray structure of P. falciparum DHODH bound to a potent and selective N-phenylbenzamide-based inhibitor (DSM59) is described at 2.3 Å resolution. The structure elucidates novel binding-site interactions and shows how conformational flexibility of the enzyme leads to the ability to bind diverse chemical structures with high affinity. This information provides new insight into the design of high-affinity DHODH inhibitors for the treatment of malaria.

PubMed: 25945708
DOI: 10.1107/S2053230X15000989

実験手法

X-RAY DIFFRACTION (2.2 Å)