High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.

Abstract:

:The fucosyltransferase NodZ is involved in the biosynthesis of the nodulation factor in nitrogen-fixing symbiotic bacteria. It catalyzes alpha1,6 transfer of l-fucose from GDP-fucose to the reducing residue of the synthesized Nod oligosaccharide. We present the structure of the NodZ protein from Bradyrhizobium expressed in Escherichia coli and crystallized in the presence of phosphate ions in two crystal forms. The enzyme is arranged into two domains of nearly equal size. Although NodZ falls in one broad class (GT-B) with other two-domain glycosyltransferases, the topology of its domains deviates from the canonical Rossmann fold, with particularly high distortions in the N-terminal domain. Mutational data combined with structural and sequence alignments indicate residues of potential importance in GDP-fucose binding or in the catalytic mechanism. They are all clustered in three conserved sequence motifs located in the C-terminal domain.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Brzezinski K,Stepkowski T,Panjikar S,Bujacz G,Jaskolski M

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

537-49

issue

3

eissn

0001-527X

issn

1734-154X

pii

20071502

journal_volume

54

pub_type

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