2hlh

Crystal structure of fucosyltransferase NodZ from Bradyrhizobium

spinqualitylabelsall models 2hlh, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hlh is a 1 chain structure with sequence from Bradyrhizobium sp. WM9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9AQ17_BRASW Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NodS

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