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The crystal structure of fructose‐1,6‐bisphosphate aldolase from Drosophila melanogaster at 2.5A˚resolution
Author(s) -
G. Hester,
O. BrennerHolzach,
Franco Antonio Rossi,
Martina Struck-Donatz,
Kaspar H. Winterhalter,
Jacques Smit,
Klaus Piontek
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80875-4
Subject(s) - aldolase a , fructose bisphosphate aldolase , drosophila melanogaster , crystal structure , crystallography , molecular replacement , melanogaster , chemistry , aldolase b , biology , enzyme , biochemistry , gene
The structure of fructose‐1,6‐bisphosphate aldolase from Drosophila melanogaster has been determined by X‐ray diffraction at 2.5A˚resolution. The insect enzyme crystallizes in space group P 2 1 2 1 2 1 with lattice constants a =86.60, b =116.80, c =151.58A˚. Molecular 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 2.5A˚, 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.