Plasmodium Falciparum Triosephosphate Isomerase-Phosphoglycolate Complex

Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state

Triosephosphate isomerase from Plasmodium falciparum: Crystal structure provides insights into antimalarial drug design

TIM; triose-phosphate isomerase; triose phosphate isomerase

MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSA
EIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNV
ILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM

12% to 25% PEG 6000 or PEG 4000 or PEG 3350 or PEG 1450 in the presence of EDTA, DTT and Sodium azide in 100mM MES. pH 6.5, VAPOR DIFFUSION, HANGING DROP at 295K

Loop Closed form of the PfTIM-Phosphoglycolate complex

RESOLUTION DEPENDENT WEIGHTING SCHEME, BULK SOLVENT MODEL USED
Grouped B factor for main chain and side chain atom of individual residues

FOUR FOLD NCS RESTRAINTS BETWEEN MONOMERS APPLIED

Triosephosphate Isomerase; Phosphoglycolate; Loop Dynamics; Loop Open Conformation, ISOMERASE

MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSA
EIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNV
ILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM