Crystal structure of mature ThnT with a covalently bound product mimic

Autoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and Catalysis.

MGSSHHHHHHSSGLVPRGSHMDPEAGSRARGLKGVHRVSANSGGIGGVPGPHNGLTDVPGVRVGHAGRTGDGWLTGVTVV
LAPPGGAVAAVDVRGGGPGTRETDALDPRNLVQTIDAVVLTGGSAFGLDAAGGVAAWLEEQGRGFPVGADPSQVVPVVPA
AALFDLGRGGTWRARPDAALGRAAVEAAAARPEGDPVEQGGVGAGTGAVVGGLKGGIGTASVVLDSGATVAALAAVNAAG
SAVDPATGVLYGARTGLPGEFAGYGVPDAIGADTHARARARLAEAAEETARRRAGGAATLNTTLAVVATDATLTRAQAQK
LAGTAHDGLARAVRPVHLLSDGDTVFALSTGRRPLLPDRPDATAARAFGVHLEAGALNEVLAAGADVLTRAVVHAVLAAT
GVDTPGGVHPSYRELYARP

15% PEG3350, 0.5M NaAcetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY

DOM-fold, amidohydrolase, autoproteolytic, carbapenem, pantetheine, inhibitor, DmpA/OAT superfamily, Pantetheine hydrolase, thienamycin biosynthesis, O-(2-oxo-4-pantoamindobutyl)threonine, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex

MDPEAGSRARGLKGVHRVSANSGGIGGVPGPHNGLTDVPGVRVGHAGRTGDGWLTGVTVVLAPPGGAVAAVDVRGGGPGT
RETDALDPRNLVQTIDAVVLTGGSAFGLDAAGGVAAWLEEQGRGFPVGADPSQVVPVVPAAALFDLGRGGTWRARPDAAL
GRAAVEAAAARPEGDPVEQGGVGAGTGAVVGGLKGGIGTASVVLDSGATVAALAAVNAAGSAVDPATGVLYGARTGLPGE
FAGYGVPDAIGADTHARARARLAEAAEETARRRAGGAATLNTTLAVVATDATLTRAQAQKLAGTAHDGLARAVRPVHLLS
DGDTVFALSTGRRPLLPDRPDATAARAFGVHLEAGALNEVLAAGADVLTRAVVHAVLAATGVDTPGGVHPSYRELYARP