Crystal structure of the F337L mutation of Trypanosoma cruzi glucokinase in the apo form (open conformation)

MGRGSHHHHHHGMAMNIKELSLHELCEELKTPAWNVPLTFVGDVGGTSARMGFVREGKNDSVHACVTRYSMKRKDITELI
EFFNEIIELMPASVIKRVKAGVINVPGPVTGGAVGGPFNNLKGIARLSDYPKALFPPGRSAILNDLEAGGFGVLAVSDAH
VFSEYFGVMWEGTQWRTCEQEPAGSVIGRGRCLVLAPGTGLGSSLIYYNPMNQQHIVVPLELGSQTIPMRKDIDYIQTLH
AELKLLPNYENMVSGAGLEFHYRQVVRGSRPPCSAGEIAKLASEGDANACKAMKKYHEYLMRVGSEASMALLPLTIVLVG
DNIVNNAFFYRNPQNLKEMHREALNHEMERLGFQSRVTYLRQKKLLNLNLMGCYRCGLDLS

1.0 uL of 7.4 mg/mL TcGlcK(F337L) in buffered solution [50 mM HEPES (pH 7.5), 0.2 M imidazole, 2 mM magnesium chloride] + 1.0 uL of precipitant solution [14% (w/v) PEG 3350, 0.1 M sodium citrate tribasic] was equilibrated against 85 uL of the precipitant solution using a 96-well sitting-drop plate (Innovadyne)

University of South Carolina, Office of the Vice President for Research, Magellan Program

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

Trypanosoma cruzi, Chagas disease, TRANSFERASE

MNIKELSLHELCEELKTPAWNVPLTFVGDVGGTSARMGFVREGKNDSVHACVTRYSMKRKDITELIEFFNEIIELMPASV
IKRVKAGVINVPGPVTGGAVGGPFNNLKGIARLSDYPKALFPPGRSAILNDLEAGGFGVLAVSDAHVFSEYFGVMWEGTQ
WRTCEQEPAGSVIGRGRCLVLAPGTGLGSSLIYYNPMNQQHIVVPLELGSQTIPMRKDIDYIQTLHAELKLLPNYENMVS
GAGLEFHYRQVVRGSRPPCSAGEIAKLASEGDANACKAMKKYHEYLMRVGSEASMALLPLTIVLVGDNIVNNAFFYRNPQ
NLKEMHREALNHEMERFGFQSRVTYLRQKKLLNLNLMGCYRCGLDLS