1b2p
From Proteopedia
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'''NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION''' | '''NATIVE MANNOSE-SPECIFIC BULB LECTIN FROM SCILLA CAMPANULATA (BLUEBELL) AT 1.7 ANGSTROMS RESOLUTION''' | ||
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[[Category: Wood, S D.]] | [[Category: Wood, S D.]] | ||
[[Category: Wright, L M.]] | [[Category: Wright, L M.]] | ||
| - | [[Category: | + | [[Category: Aglutinin]] |
| - | [[Category: | + | [[Category: Bluebell bulb]] |
| - | [[Category: | + | [[Category: Mannose-binding lectin]] |
| - | [[Category: | + | [[Category: Monocot]] |
| - | [[Category: | + | [[Category: Protein- carbohydrate interaction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:59:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:59, 2 May 2008
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 Page seeded by OCA on Fri May 2 10:59:04 2008
