Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, FBP-bound form

Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.

Fructose-1,6-bisphosphate aldolase/phosphatase

MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEV
TDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDP
SMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVR
AQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDL
FDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTALPKILAKVKPYPADQYEKDRKKYIEAVVKGAKVEESQHDL
EHHHHHH

8% PEG3350, 0.1 M HEPES/NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, ligand free

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, F6P-bound form

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, soaked with EDTA and DHAP

Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, Y229F variant with DHAP

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY

(beta/alpha)8 TIM barrel, FBP, F6P, DHAP, GAP, phosphorylation, LYASE, HYDROLASE

MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEV
TDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDP
SMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVR
AQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDL
FDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTALPKILAKVKPYPADQYEKDRKKYIEAVVKGAKVEESQHD