ArticleProtein science : a publication of the Protein Society2004
An improved crystal form of Plasmodium falciparum peptide deformylase.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Drug Repurposing and Polypharmacology to Fight SARS-CoV-2 Through Inhibition of the Main Protease.Frontiers in pharmacology · 2021Article
- Discovery of Potential Plant-Derived Peptide Deformylase (PDF) Inhibitors for Multidrug-Resistant Bacteria Using Computational Studies.Journal of clinical medicine · 2018Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
- High tolerance to mutations in a Chlamydia trachomatis peptide deformylase loop.World journal of biological chemistry · 2011Article
- Trapping conformational states along ligand-binding dynamics of peptide deformylase: the impact of induced fit on enzyme catalysis.PLoS biology · 2011Article
- Application of protein engineering to enhance crystallizability and improve crystal properties.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase (PDF) from Bacillus cereus in ligand-free and actinonin-bound forms.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
An altered version of peptide deformylase from Plasmodium falciparum (PfPDF), the organism that causes the most devastating form of malaria, has been cocrystallized with a synthesized inhibitor that has submicromolar affinity for its target protein. The structure is solved at 2.2 A resolution, an improvement over the 2.8 A resolution achieved during the structural determination of unliganded PfPDF. This represents the successful outcome of modifying the protein construct in order to overcome adverse crystal contacts and other problems encountered in the study of unliganded PfPDF. Two molecules of PfPDF are found in the asymmetric unit of the current structure. The active site of each monomer of PfPDF is occupied by a proteolyzed fragment of the tripeptide-like inhibitor. Unexpectedly, each PfPDF subunit is associated with two nearly complete molecules of the inhibitor, found at a protein-protein interface. This is the first structure of a eukaryotic PDF protein, a potential drug target, in complex with a ligand.
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