Structure of C126S mutant of Plasmodium falciparum triosephosphate isomerase

Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability.

MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSA
EIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVSFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNV
ILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM

24% PEG, 1M HEPES bufffer (pH 7.0), 10mM Lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSA
EIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNV
ILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM