1JYM

Crystals of Peptide Deformylase from Plasmodium falciparum with Ten Subunits per Asymmetric Unit Reveal Critical Characteristics of the Active Site for Drug Design

1JYM の概要

• エントリーDOI: 10.2210/pdb1jym/pdb
• 分子名称: Peptide Deformylase, COBALT (II) ION (3 entities in total)
• 機能のキーワード: pdf, malaria, plasmodium, deformylation, metalloenzyme, hydrolase
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 218807.53

構造登録者

Kumar, A.,Nguyen, K.T.,Srivathsan, S.,Ornstein, B.,Turley, S.,Hirsh, I.,Pei, D.,Hol, W.G.J. (登録日: 2001-09-12, 公開日: 2002-03-13, 最終更新日: 2024-10-30)

主引用文献

Kumar, A.,Nguyen, K.T.,Srivathsan, S.,Ornstein, B.,Turley, S.,Hirsh, I.,Pei, D.,Hol, W.G.
Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design.
Structure, 10:357-367, 2002

PubMed Abstract: Peptide deformylase catalyzes the deformylation reaction of the amino terminal fMet residue of newly synthesized proteins in bacteria, and most likely in Plasmodium falciparum, and has therefore been identified as a potential antibacterial and antimalarial drug target. The structure of P. falciparum peptide deformylase, determined at 2.8 A resolution with ten subunits per asymmetric unit, is similar to the bacterial enzyme with the residues involved in catalysis, the position of the bound metal ion, and a catalytically important water structurally conserved between the two enzymes. However, critical differences in the substrate binding region explain the poor affinity of E. coli deformylase inhibitors and substrates toward the Plasmodium enzyme. The Plasmodium structure serves as a guide for designing novel antimalarials.

PubMed: 12005434
DOI: 10.1016/S0969-2126(02)00719-0

実験手法

X-RAY DIFFRACTION (2.8 Å)