1FUI

L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI

Summary for 1FUI

• Entry DOI: 10.2210/pdb1fui/pdb
• Descriptor: L-FUCOSE ISOMERASE, MANGANESE (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: isomerase, ketol isomerase, fucose metabolism, l-fucose to l-fuculose conversion
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P69922
• Total number of polymer chains: 6
• Total formula weight: 391761.13

Authors

Seemann, J.E.,Schulz, G.E. (deposition date: 1997-04-14, release date: 1997-10-15, Last modification date: 2024-02-07)

Primary citation

Seemann, J.E.,Schulz, G.E.
Structure and mechanism of L-fucose isomerase from Escherichia coli.
J.Mol.Biol., 273:256-268, 1997

PubMed Abstract: The three-dimensional structure of L-fucose isomerase from Escherichia coli has been determined by X-ray crystallography at 2.5 A resolution. This ketol isomerase converts the aldose L-fucose into the corresponding ketose L-fuculose using Mn2+ as a cofactor. Being a hexamer with 64,976 Da per subunit, L-fucose isomerase is the largest structurally known ketol isomerase. The enzyme shows neither sequence nor structural similarity with other ketol isomerases. The hexamer obeys D3 symmetry and forms the crystallographic asymmetric unit. The strict and favorably oriented local symmetry allowed for a computational phase extension from 7.3 A to 2.5 A resolution. The structure was solved with an L-fucitol molecule bound to the catalytic center such that the hydroxyl groups at positions 1 and 2 are ligands of the manganese ion. Most likely, L-fucitol mimics a bound L-fucose molecule in its open chain form. The protein environment suggests strongly that the reaction belongs to the ene-diol type.

PubMed: 9367760
DOI: 10.1006/jmbi.1997.1280

Experimental method

X-RAY DIFFRACTION (2.5 Å)