PDBsum entry 2hhc

Transferase

PDB id

2hhc

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Contents

			Protein chain

					291 a.a. *

			Ligands

					PO4 ×3


					TRS

			Waters ×323

* Residue conservation analysis

PDB id:

2hhc

Links

Name:

Transferase

Title:

Crystal structure of fucosyltransferase nodz from bradyrhizobium

Structure:

Nodulation fucosyltransferase nodz. Chain: a. Synonym: nodz. Engineered: yes

Source:

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

Resolution:

1.54Å

R-factor:

0.183

R-free:

0.197

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:

28-Jun-06

Release date:

17-Jul-07

PROCHECK

	Headers

	References

Protein chain

Q9AQ17 (Q9AQ17_BRASW) - Nodulation fucosyltransferase NodZ from Bradyrhizobium sp. (strain WM9)

Seq: Struc:					324 a.a. 291 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.4.1.- - ?????

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20466647

H.Ihara, S.Hanashima, T.Okada, R.Ito, Y.Yamaguchi, N.Taniguchi, and Y.Ikeda (2010).
Fucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure.

Glycobiology, 20, 1021-1033.

20466652

L.Zhang, K.Lau, J.Cheng, H.Yu, Y.Li, G.Sugiarto, S.Huang, L.Ding, V.Thon, P.G.Wang, and X.Chen (2010).
Helicobacter hepaticus Hh0072 gene encodes a novel alpha1-3-fucosyltransferase belonging to CAZy GT11 family.

Glycobiology, 20, 1077-1088.

18822375

B.Henrissat, G.Sulzenbacher, and Y.Bourne (2008).
Glycosyltransferases, glycoside hydrolases: surprise, surprise!

Curr Opin Struct Biol, 18, 527-533.

19052372

O.Cakici, M.Sikorski, T.Stepkowski, G.Bujacz, and M.Jaskolski (2008).
Cloning, expression, purification, crystallization and preliminary X-ray analysis of NodS N-methyltransferase from Bradyrhizobium japonicum WM9.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1149-1152.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.