2bl4

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spinqualitylabelsall models 2bl4, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI

Overview

The FucO protein, a member of the group III "iron-activated", dehydrogenases, catalyzes the interconversion between L-lactaldehyde and, L-1,2-propanediol in Escherichia coli. The three-dimensional structure of, FucO in a complex with NAD(+) was solved, and the presence of iron in the, crystals was confirmed by X-ray fluorescence. The FucO structure presented, here is the first structure for a member of the group III bacterial, dehydrogenases shown experimentally to contain iron. FucO forms a dimer, in which each monomer folds into an alpha/beta dinucleotide-binding, N-terminal domain and an all-alpha-helix C-terminal domain that are, separated by a deep cleft. The dimer is formed by the swapping (between, monomers) of the first chain of the beta-sheet. The binding site for, Fe(2+) is ... [(full description)]

About this Structure

2BL4 is a [Single protein] structure of sequence from [Escherichia coli] with FE2, CL and NAD as [ligands]. Active as [Lactaldehyde reductase], with EC number [1.1.1.77]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli., Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J, J Bacteriol. 2005 Jul;187(14):4957-66. PMID:15995211

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