Structural change of FBP aldolase/phosphatase

FBP aldolase/phosphatase is an amazing enzyme that can catalyze two chemically distinct reactions. This enzyme is exclusively possessed by a group of archaeal and thermophilic microbes and is thought to be a remnant of a primordial sugar biosynthetic pathway. A dramatic structural change in the active site (enzyme metamorphosis) was revealed by detemining two crystal strucures (FBP aldolase and FBP phosphatase forms).

	Name	State / change	Note
	E	Full open (Aldolase)
		+ DHAP (yellow) + 3 Mg2+ (magenta)	Shiff Base loop (yellow) open
	E:DHAP:3 Mg2+	Aldolase form (DHAP Schiff Base)	3RIM
		+ GA3P (green)
	E:DHAP:GA3P:3 Mg2+	Aldolase form (Ternary complex)
		Aldolase reaction	DHAP + GA3P FBP (cyan)
	E:FBP:3 Mg2+	Aldolase form (FBP complex)
		Enzyme metamorphosis + 1 Mg2+ (magenta)	Shiff Base loop (yellow) open Lid loop (blue) close C term. loop (pink) close
	E:FBP:4 Mg2+	Phosphatase form (FBP complex)	1UMG
		Phosphatase reaction	FBP F6P (grey) + Pi (orange)
	E:F6P:Pi:4 Mg2+	Phosphatase form (product complex)
		- F6P - Pi - 4 Mg2+	Lid loop (blue) open C term. loop (pink) open
	E	Full open (Phosphatase)

High quality QuickTime movie (11.9 MB) is here.

This movie is created by estimating intermediate states from the two crystal structures (aldolase-DHAP Schiff Base and phosphatase-FBP complex) by a simple method. It does not represent the real intermediate states.

For details, see our articles on Structure and Nature.

Nishimasu et al., Structure 12 (6), 949-959 (2004)

Fushinobu et al., Nature 43 (7370), 538-541 (2011)

S. Fushinobu, H. Nishimasu, and T. Wakagi