1B2P

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

Summary for 1B2P

• Entry DOI: 10.2210/pdb1b2p/pdb
• Descriptor: PROTEIN (LECTIN) (2 entities in total)
• Functional Keywords: mannose-binding lectin, monocot, aglutinin, bluebell bulbs, protein- carbohydrate interactions, sugar binding protein
• Biological source: Hyacinthoides hispanica
• Total number of polymer chains: 2
• Total formula weight: 26419.71

Authors

Wood, S.D.,Wright, L.M.,Reynolds, C.D.,Rizkallah, P.J.,Allen, A.K.,Peumans, W.J.,Van Damme, E.J.M. (deposition date: 1998-11-30, release date: 1999-07-22, Last modification date: 2023-08-09)

Primary citation

Wood, S.D.,Wright, L.M.,Reynolds, C.D.,Rizkallah, P.J.,Allen, A.K.,Peumans, W.J.,Van Damme, E.J.
Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 A resolution.
Acta Crystallogr.,Sect.D, 55:1264-1272, 1999

PubMed Abstract: 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.

PubMed: 10393293
DOI: 10.1107/S0907444999005326

Experimental method

X-RAY DIFFRACTION (1.7 Å)