Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.

Mechanism of the Schiff Base Forming Fructose-1,6-Bisphosphate Aldolase: Structural Analysis of Reaction Intermediates.

K177 COVALENTLY LINKED TO THE CARBINOLAMINE FORM OF THE SUBSTRATE FBP

FRUCTOSE-BIPHOSPHATE ALDOLASE CLASS I, FBP ALDOLASE

MANLTEKFLRIFARRGKSIILAYDHGIEHGPADFMDNPDSADPEYILRLARDAGFDGVVFQRGIAEKYYDGSVPLILKLN
GKTTLYNGEPVSVANCSVEEAVSLGASAVGYTIYPGSGFEWKMFEELARIKRDAVKFDLPLVVWSFPRGGKVVNETAPEI
VAYAARIALELGSDAMKIKYTGDPKTFSWAVKVAGKVPVLMSGGPKTKTEEDFLKQVEGVLEAGALGIAVGRNVWQRRDA
LKFARALAELVYGGKKLAEPLNV

SOLVED BY RIGID BODY REFINEMENT OF 1OJX.

9% (W/V) PEG 4000, 0.1 M NAACETATE PH 5.0, 1-8% GLYCEROL, 100 MM FBP

ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE

CRYSTAL STRUCTURE OF AN ARCHAEAL FRUCTOSE 1,6- BISPHOSPHATE ALDOLASE

ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6 -BISPHOSPHATE ALDOLASE

THE MECHANISM OF THE SCHIFF BASE FORMING FRUCTOSE-1, 6-BISPHOSPHATE ALDOLASE: STRUCTURAL ANALYSIS OF REACTION INTERMEDIATES.

ENGINEERED RESIDUE IN CHAIN A, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN A, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN B, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN B, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN C, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN C, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN D, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN D, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN E, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN E, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN F, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN F, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN G, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN G, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN H, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN H, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN I, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN I, ALA 173 TO SER ENGINEERED RESIDUE IN CHAIN J, TYR 146 TO PHE ENGINEERED RESIDUE IN CHAIN J, ALA 173 TO SER
M2P: THE SUBSTRATE FRUCTOSE 1,6-BISPHOSPHATE IS COVALENTLY LINKED TO THE CATALYTIC LYSINE AS A CARBINOLAMINE FORM.

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