2hlh

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[[Image:2hlh.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2hlh| PDB=2hlh | SCENE= }}
{{STRUCTURE_2hlh| PDB=2hlh | SCENE= }}
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'''Crystal structure of fucosyltransferase NodZ from Bradyrhizobium'''
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===Crystal structure of fucosyltransferase NodZ from Bradyrhizobium===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 17762900 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17762900}}
==About this Structure==
==About this Structure==
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[[Category: Nodulation]]
[[Category: Nodulation]]
[[Category: Nodz]]
[[Category: Nodz]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:25:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:29:49 2008''

Revision as of 00:30, 28 July 2008

Image:2hlh.png

Template:STRUCTURE 2hlh

Crystal structure of fucosyltransferase NodZ from Bradyrhizobium

Template:ABSTRACT PUBMED 17762900

About this Structure

2HLH 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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