1RQC

Crystals of peptide deformylase from Plasmodium falciparum with ten subunits per asymmetric unit reveal critical characteristics of the active site for drug design

Summary for 1RQC

• Entry DOI: 10.2210/pdb1rqc/pdb
• Related: 1JYM 1RL4
• Descriptor: formylmethionine deformylase, COBALT (II) ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Plasmodium falciparum (malaria parasite P. falciparum)
• Total number of polymer chains: 10
• Total formula weight: 221069.82

Authors

Robien, M.A.,Nguyen, K.T.,Kumar, A.,Hirsh, I.,Turley, S.,Pei, D.,Hol, W.G. (deposition date: 2003-12-04, release date: 2004-01-20, Last modification date: 2024-10-30)

Primary citation

Robien, M.A.,Nguyen, K.T.,Kumar, A.,Hirsh, I.,Turley, S.,Pei, D.,Hol, W.G.
An improved crystal form of Plasmodium falciparum peptide deformylase
Protein Sci., 13:1155-1163, 2004

PubMed 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.

PubMed: 15010544
DOI: 10.1110/ps.03456404

Experimental method

X-RAY DIFFRACTION (2.8 Å)