1iqb

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Revision as of 18:27, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1iqb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iqb, resolution 1.90Å" /> '''Crystal Structure of...)
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File:1iqb.jpg


1iqb, resolution 1.90Å

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Crystal Structure of Urtica dioica Agglutinin Isolectin I

OverviewOverview

Ultica dioica agglutinin, a plant lectin from the stinging nettle, consists of a total of seven individual isolectins. One of these, structures, isolectin I, was determined at 1.9 A resolution by the X-ray, method. The crystals belong to the space group P2(1) and the asymmetric, unit contains two molecules related by local twofold symmetry. The, molecule consists of two hevein-like chitin-binding domains lacking, distinct secondary structure, but four disulfide bonds in each domain, maintain the tertiary structure. The backbone structure of the two, independent molecules is essentially identical and this is similarly true, of the sugar-binding sites. In the crystal, the C-terminal domains bind, Zn(2+) ions at the sugar-binding site. Owing to their location near a, pseudo-twofold axis, the two zinc ions link the two independent molecules, in a tail-to-tail arrangement: thus, His47 of molecule 1 and His67 of, molecule 2 coordinate the first zinc ion, while the second zinc ion links, Asp75 of molecule 1 and His47 of molecule 2.

About this StructureAbout this Structure

1IQB is a Single protein structure of sequence from Urtica dioica with ZN as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Urtica dioica agglutinin isolectin I: dimer formation mediated by two zinc ions bound at the sugar-binding site., Harata K, Schubert WD, Muraki M, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1513-7. Epub 2001, Oct 25. PMID:11679714

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