PDBsum entry: 2hlh

Transferase

PDB-id: 2hlh

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

286 a.a. *

Ligands

PO4 ×4

Waters ×280

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

2hlh

Name:

Transferase

Title:

Crystal structure of fucosyltransferase nodz from bradyrhizobium

Structure:

Nodulation fucosyltransferase. Chain: a. Engineered: yes

Source:

Bradyrhizobium sp. Wm9. Organism_taxid: 133505. Strain: wm9. Gene: nodz. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

Q9AQ17 (Q9AQ17_BRASW)

Seq:

Struc:

Seq:

324 a.a.

Struc:

286 a.a.

Key:

PfamA domain

Secondary structure

Resolution:

1.95Å

R-factor:

0.162

R-free:

0.206

Authors:

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

Key ref:

K.Brzezinski et al. (2007). High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.. Acta Biochim Pol, 54, 537-549. [PubMed id: 17762900]

Date:

07-Jul-06

Release date:

17-Jul-07

Related entries:

2hhc
crystal structure of fucosyltransferase nodz from
bradyrhizobium

Quick_links

Procheck

Clefts

Surface

Key reference

Acta Biochim Pol 54:537-549 (2007)

PubMed id: 17762900

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

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

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.