1ouw
From Proteopedia
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|PDB= 1ouw |SIZE=350|CAPTION= <scene name='initialview01'>1ouw</scene>, resolution 1.37Å | |PDB= 1ouw |SIZE=350|CAPTION= <scene name='initialview01'>1ouw</scene>, resolution 1.37Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MLT:MALATE+ION'>MLT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1c3k|1C3K]], [[1c3m|1C3M]], [[1c3n|1C3N]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ouw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouw OCA], [http://www.ebi.ac.uk/pdbsum/1ouw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ouw RCSB]</span> | ||
}} | }} | ||
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[[Category: Roig-Zamboni, V.]] | [[Category: Roig-Zamboni, V.]] | ||
[[Category: Rouge, P.]] | [[Category: Rouge, P.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: IMD]] | ||
| - | [[Category: MLT]] | ||
[[Category: agglutinin]] | [[Category: agglutinin]] | ||
[[Category: beta-prism fold]] | [[Category: beta-prism fold]] | ||
| Line 38: | Line 38: | ||
[[Category: mannose-binding]] | [[Category: mannose-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:40 2008'' |
Revision as of 19:50, 30 March 2008
| |||||||
| , resolution 1.37Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1C3K, 1C3M, 1C3N
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Calystegia sepium agglutinin
Overview
The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same beta-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded beta-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the beta-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
About this Structure
1OUW is a Single protein structure of sequence from Calystegia sepium. Full crystallographic information is available from OCA.
Reference
The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold., Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P, J Biol Chem. 2004 Jan 2;279(1):527-33. Epub 2003 Oct 15. PMID:14561768
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