Structural highlights
Function
[FUCI_ECOLI] Converts the aldose L-fucose into the corresponding ketose L-fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively.[HAMAP-Rule:MF_01254]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure and mechanism of L-fucose isomerase from Escherichia coli.,Seemann JE, Schulz GE J Mol Biol. 1997 Oct 17;273(1):256-68. PMID:9367760[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seemann JE, Schulz GE. Structure and mechanism of L-fucose isomerase from Escherichia coli. J Mol Biol. 1997 Oct 17;273(1):256-68. PMID:9367760 doi:http://dx.doi.org/10.1006/jmbi.1997.1280
