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Structure and mechanism of L-fucose isomerase from Escherichia coli.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Seemann JE,Schulz GE

doi

10.1006/jmbi.1997.1280

subject

Has Abstract

pub_date

1997-10-17 00:00:00

pages

256-68

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(97)91280-8

journal_volume

273

pub_type

杂志文章

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