1rl4
Plasmodium falciparum peptide deformylase complex with inhibitorPlasmodium falciparum peptide deformylase complex with inhibitor
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAn 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. An improved crystal form of Plasmodium falciparum peptide deformylase.,Robien MA, Nguyen KT, Kumar A, Hirsh I, Turley S, Pei D, Hol WG Protein Sci. 2004 Apr;13(4):1155-63. Epub 2004 Mar 9. PMID:15010544[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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