6DSS

Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase

6DSS の概要

• エントリーDOI: 10.2210/pdb6dss/pdb
• 分子名称: Orotidine 5'-monophosphate decarboxylase, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: complex, p falciparum, lyase
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76380.85

構造登録者

Brandt, G.S.,Novak, W.R.P. (登録日: 2018-06-14, 公開日: 2018-10-17, 最終更新日: 2023-10-11)

主引用文献

Novak, W.R.P.,West, K.H.J.,Kirkman, L.M.D.,Brandt, G.S.
Re-refinement of Plasmodium falciparum orotidine 5'-monophosphate decarboxylase provides a clearer picture of an important malarial drug target.
Acta Crystallogr F Struct Biol Commun, 74:664-668, 2018

PubMed Abstract: The development of antimalarial drugs remains a public health priority, and the orotidine 5'-monophosphate decarboxylase from Plasmodium falciparum (PfOMPDC) has great potential as a drug target. The crystallization of PfOMPDC with substrate bound represents an important advance for structure-based drug-design efforts [Tokuoka et al. (2008), J. Biochem. 143, 69-78]. The complex of the enzyme bound to the substrate OMP (PDB entry 2za1) would be of particular utility in this regard. However, re-refinement of this structure of the Michaelis complex shows that the bound ligand is the product rather than the substrate. Here, the re-refinement of a set of three structures, the apo enzyme and two versions of the product-bound form (PDB entries 2za1, 2za2 and 2za3), is reported. The improved geometry and fit of these structures to the observed electron density will enhance their utility in antimalarial drug design.

PubMed: 30279319
DOI: 10.1107/S2053230X18010610

実験手法

X-RAY DIFFRACTION (2.599 Å)