2ocx

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(New page: 200px<br /><applet load="2ocx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ocx, resolution 2.20&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: nodz]]
[[Category: nodz]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:21:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:59 2008''

Revision as of 16:17, 21 February 2008


2ocx, resolution 2.20Å

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Crystal structure of Se-Met fucosyltransferase NodZ from Bradyrhizobium

Overview

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.

About this Structure

2OCX is a Single protein structure of sequence from Bradyrhizobium sp. with and as ligands. Active as Glycoprotein 6-alpha-L-fucosyltransferase, with EC number 2.4.1.68 Full crystallographic information is available from OCA.

Reference

High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor., Brzezinski K, Stepkowski T, Panjikar S, Bujacz G, Jaskolski M, Acta Biochim Pol. 2007;54(3):537-49. Epub 2007 Aug 30. PMID:17762900

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