The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.
The structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been determined by X-ray diffraction at 2.5 A resolution. The insect enzyme crystallizes in space group P2(1)2(1)2(1) with lattice replacement with rabbit muscle aldolase as a search model has been employed to solve the structure. To improve the initial phases real space averaging, including phase extension from 4.0 to 2.5 A, has been applied. Refinement of the atomic positions by molecular dynamics resulted in a crystallographic R-factor of 0.214. The tertiary structure resembles in most parts that of the vertebrate aldolase from rabbit muscle. Significant differences were found in surface loops and the N- and C-terminal regions of the protein. Here we present the first aldolase structure where the functionally important C-terminal arm is described completely.
Hester
G
G
Laboratorium für Biochemie I, Eidgenössische Technische Hochschule Zürich, Switzerland.
Brenner-Holzach
O
O
Rossi
F A
FA
Struck-Donatz
M
M
Winterhalter
K H
KH
Smit
J D
JD
Piontek
K
K
D000818:Animals; D003460:Crystallization; D004331:Drosophila melanogaster / Q000201:enzymology; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry*; D007313:Insecta; D011487:Protein Conformation; D011817:Rabbits; D014961:X-Ray Diffraction
D005634:Fructose-Bisphosphate Aldolase