2HHC

Crystal structure of fucosyltransferase NodZ from Bradyrhizobium

2HHC の概要

• エントリーDOI: 10.2210/pdb2hhc/pdb
• 分子名称: Nodulation fucosyltransferase NodZ, PHOSPHATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, fucosyltransferase, nodz, nodulation, transferase
• 由来する生物種: Bradyrhizobium sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38236.04

構造登録者

Brzezinski, K.,Stepkowski, T.,Panjikar, S.,Bujacz, G.,Jaskolski, M. (登録日: 2006-06-28, 公開日: 2007-07-17, 最終更新日: 2024-03-13)

主引用文献

Brzezinski, K.,Stepkowski, T.,Panjikar, S.,Bujacz, G.,Jaskolski, M.
High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.
Acta Biochim.Pol., 54:537-549, 2007

PubMed 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.

PubMed: 17762900

実験手法

X-RAY DIFFRACTION (1.54 Å)