2hhc

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|PDB= 2hhc |SIZE=350|CAPTION= <scene name='initialview01'>2hhc</scene>, resolution 1.54&Aring;
|PDB= 2hhc |SIZE=350|CAPTION= <scene name='initialview01'>2hhc</scene>, resolution 1.54&Aring;
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+A+1002'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+1003'>AC3</scene> and <scene name='pdbsite=AC4:Trs+Binding+Site+For+Residue+A+2001'>AC4</scene>
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+A+1002'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+1003'>AC3</scene> and <scene name='pdbsite=AC4:Trs+Binding+Site+For+Residue+A+2001'>AC4</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
+
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= nodZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=376 Bradyrhizobium sp.])
|GENE= nodZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=376 Bradyrhizobium sp.])
 +
|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhc OCA], [http://www.ebi.ac.uk/pdbsum/2hhc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hhc RCSB]</span>
}}
}}
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[[Category: Panjikar, S.]]
[[Category: Panjikar, S.]]
[[Category: Stepkowski, T.]]
[[Category: Stepkowski, T.]]
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[[Category: PO4]]
 
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[[Category: TRS]]
 
[[Category: fucosyltransferase]]
[[Category: fucosyltransferase]]
[[Category: glycosyltransferase]]
[[Category: glycosyltransferase]]
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[[Category: nodz]]
[[Category: nodz]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:30:25 2008''

Revision as of 00:30, 31 March 2008


PDB ID 2hhc

Drag the structure with the mouse to rotate
, resolution 1.54Å
Sites: , , and
Ligands: ,
Gene: nodZ (Bradyrhizobium sp.)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of 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

2HHC is a Single protein structure of sequence from Bradyrhizobium sp.. 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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