2ZA3

Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with uridine 5'-monophosphate from P.falciparum

2ZA3 の概要

• エントリーDOI: 10.2210/pdb2za3/pdb
• 関連するPDBエントリー: 2F84 2ZA1 2ZA2
• 分子名称: Orotidine 5'-phosphate decarboxylase, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: orotidine 5'-monophosphate decarboxylase, plasmodium falciparum, uridine 5'-monophosphate, lyase, pyrimidine biosynthesis
• 由来する生物種: Plasmodium falciparum (malaria parasite P. 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

Tokuoka, K.,Inoue, T. (登録日: 2007-09-26, 公開日: 2007-12-04, 最終更新日: 2023-11-01)

主引用文献

Tokuoka, K.,Kusakari, Y.,Krungkrai, S.R.,Matsumura, H.,Kai, Y.,Krungkrai, J.,Horii, T.,Inoue, T.
Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase
J.Biochem.(Tokyo), 143:69-78, 2008

PubMed Abstract: Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 A, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.

PubMed: 17981823
DOI: 10.1093/jb/mvm193

実験手法

X-RAY DIFFRACTION (2.65 Å)