1FBA

THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION

Summary for 1FBA

• Entry DOI: 10.2210/pdb1fba/pdb
• Descriptor: FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE (2 entities in total)
• Functional Keywords: lyase(aldehyde)
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 4
• Total formula weight: 155956.72

Authors

Piontek, K.,Hester, G.,Brenner-Holzach, O. (deposition date: 1992-06-08, release date: 1993-10-31, Last modification date: 2024-10-16)

Primary citation

Hester, G.,Brenner-Holzach, O.,Rossi, F.A.,Struck-Donatz, M.,Winterhalter, K.H.,Smit, J.D.,Piontek, K.
The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution.
FEBS Lett., 292:237-242, 1991

PubMed Abstract: 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.

PubMed: 1959612
DOI: 10.1016/0014-5793(91)80875-4

Experimental method

X-RAY DIFFRACTION (1.9 Å)