5FBP

CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION

5FBP の概要

• エントリーDOI: 10.2210/pdb5fbp/pdb
• 分子名称: FRUCTOSE 1,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose (3 entities in total)
• 機能のキーワード: hydrolase (phosphoric monoester)
• 由来する生物種: Sus scrofa (pig)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73786.42

構造登録者

Ke, H.,Liang, J.-Y.,Zhang, Y.,Lipscomb, W.N. (登録日: 1991-02-11, 公開日: 1992-07-15, 最終更新日: 2024-03-13)

主引用文献

Ke, H.M.,Zhang, Y.P.,Liang, J.Y.,Lipscomb, W.N.
Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution.
Proc.Natl.Acad.Sci.USA, 88:2989-2993, 1991

PubMed Abstract: The crystal structure of fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with the product fructose 6-phosphate (F6P) has been refined at 2.1-A resolution to an R factor of 0.177 with root-mean-square deviations of 0.014 A and 2.9 degrees from the ideal geometries of bond lengths and bond angles, respectively. The secondary structures but not the trace of the unligated enzyme have been slightly revised in the F6P complex at this higher resolution. Helix H4 in the unligated structure has been refined to a helix-like coil, and two very short 3(10) helices have been found, one in H4 and one in H5. F6P at 10 mM concentration in the absence of divalent metals in our study shows major binding at the active site and minor binding at the AMP site. The major site has almost equal full occupancy in the C1 and C2 chains of the crystallographic asymmetric unit, while the minor site shows occupancy only in the C1 chain at about 50%. The electron density in both (2Fo - Fc) and (Fo - Fc) maps calculated by omitting F6P slightly favors the beta anomer of D-F6P over the alpha anomer. Possible functions of the active-site residues are discussed, and candidates are suggested for site-directed mutagenesis.

PubMed: 1849642
DOI: 10.1073/pnas.88.8.2989

実験手法

X-RAY DIFFRACTION (2.1 Å)