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1b2p

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Revision as of 21:30, 24 November 2007 by OCA (Talk | contribs)
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1b2p, resolution 1.7Å

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NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION

Overview

The X-ray crystal structure of native Scilla campanulata agglutinin, a, mannose-specific lectin from bluebell bulbs and a member of the Liliaceae, family, has been determined by molecular replacement and refined to an R, value of 0.186 at 1.7 A resolution. The lectin crystallizes in space group, P21212 with unit-cell parameters a = 70. 42, b = 92.95, c = 46.64 A. The, unit cell contains eight protein molecules of Mr = 13143 Da (119, amino-acid residues). The asymmetric unit comprises two chemically, identical molecules, A and B, related by a non-crystallographic twofold, axis perpendicular to c. This dimer further associates by crystallographic, twofold symmetry to form a tetramer. The fold of the polypeptide backbone, closely resembles that found in the lectins from Galanthus nivalis, (snowdrop) and Hippeastrum (amaryllis) and contains a threefold symmetric, beta-prism made up of three antiparallel four-stranded beta-sheets. Each, of the four-stranded beta-sheets (I, II and III) possesses a potential, saccharide-binding site containing conserved residues; however, site II, has two mutations relative to sites I and III which may prevent ligation, at this site. Our study provides the first accurate and detailed, description of a native (unligated) structure from this superfamily of, mannose-specific bulb lectins and will allow comparisons with a number of, lectin-saccharide complexes which have already been determined or are, currently under investigation.

About this Structure

1B2P is a Single protein structure of sequence from Hyacinthoides hispanica. Full crystallographic information is available from OCA.

Reference

Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 A resolution., Wood SD, Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Peumans WJ, Van Damme EJ, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1264-72. PMID:10393293

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