4C82

IspF (Plasmodium falciparum) unliganded structure

4C82 の概要

• エントリーDOI: 10.2210/pdb4c82/pdb
• 関連するPDBエントリー: 4C81 4C8E 4C8G 4C8I
• 分子名称: 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: PLASMODIUM FALCIPARUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20801.47

構造登録者

O'Rourke, P.E.F.,Kalinowska-Tluscik, J.,Fyfe, P.K.,Dawson, A.,Hunter, W.N. (登録日: 2013-09-27, 公開日: 2014-01-08, 最終更新日: 2023-12-20)

主引用文献

O Rourke, P.E.,Kalinowska-Tluscik, J.,Fyfe, P.K.,Dawson, A.,Hunter, W.N.
Crystal Structures of Ispf from Plasmodium Falciparum and Burkholderia Cenocepacia: Comparisons Inform Antimicrobial Drug Target Assessment.
Bmc Struct.Biol., 14:1-, 2014

PubMed Abstract: 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase (IspF) catalyzes the conversion of 4-diphosphocytidyl-2C-methyl-D-erythritol-2-phosphate to 2C-methyl-D-erythritol-2,4-cyclodiphosphate and cytidine monophosphate in production of isoprenoid-precursors via the methylerythritol phosphate biosynthetic pathway. IspF is found in the protozoan Plasmodium falciparum, a parasite that causes cerebral malaria, as well as in many Gram-negative bacteria such as Burkholderia cenocepacia. IspF represents a potential target for development of broad-spectrum antimicrobial drugs since it is proven or inferred as essential in these pathogens and absent from mammals. Structural studies of IspF from these two important yet distinct pathogens, and comparisons with orthologues have been carried out to generate reagents, to support and inform a structure-based approach to early stage drug discovery.

PubMed: 24410837
DOI: 10.1186/1472-6807-14-1

実験手法

X-RAY DIFFRACTION (2 Å)