2eig
From Proteopedia
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|PDB= 2eig |SIZE=350|CAPTION= <scene name='initialview01'>2eig</scene>, resolution 2.00Å | |PDB= 2eig |SIZE=350|CAPTION= <scene name='initialview01'>2eig</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+B+3001'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+A+1101'>AC3</scene>, <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+A+1102'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+B+1201'>AC5</scene>, <scene name='pdbsite=AC6:Ca+Binding+Site+For+Residue+B+1202'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+C+1301'>AC7</scene>, <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+C+1302'>AC8</scene>, <scene name='pdbsite=AC9:Mn+Binding+Site+For+Residue+D+1401'>AC9</scene> and <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+D+1402'>BC1</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+B+3001'>AC2</scene>, <scene name='pdbsite=AC3:Mn+Binding+Site+For+Residue+A+1101'>AC3</scene>, <scene name='pdbsite=AC4:Ca+Binding+Site+For+Residue+A+1102'>AC4</scene>, <scene name='pdbsite=AC5:Mn+Binding+Site+For+Residue+B+1201'>AC5</scene>, <scene name='pdbsite=AC6:Ca+Binding+Site+For+Residue+B+1202'>AC6</scene>, <scene name='pdbsite=AC7:Mn+Binding+Site+For+Residue+C+1301'>AC7</scene>, <scene name='pdbsite=AC8:Ca+Binding+Site+For+Residue+C+1302'>AC8</scene>, <scene name='pdbsite=AC9:Mn+Binding+Site+For+Residue+D+1401'>AC9</scene> and <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+D+1402'>BC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eig OCA], [http://www.ebi.ac.uk/pdbsum/2eig PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eig RCSB]</span> | ||
}} | }} | ||
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[[Category: Oliveira, T M.de.]] | [[Category: Oliveira, T M.de.]] | ||
[[Category: Vicoti, M M.]] | [[Category: Vicoti, M M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: NAG]] | ||
[[Category: l-fucosyl]] | [[Category: l-fucosyl]] | ||
[[Category: lotus tetragonolobus]] | [[Category: lotus tetragonolobus]] | ||
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[[Category: sugar binding protein]] | [[Category: sugar binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:49:35 2008'' |
Revision as of 23:49, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Lotus tetragonolobus seed lectin (Isoform)
Overview
Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.
About this Structure
2EIG is a Single protein structure of sequence from Lotus tetragonolobus. Full crystallographic information is available from OCA.
Reference
Identification of a new quaternary association for legume lectins., Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr, J Struct Biol. 2008 Feb;161(2):133-43. Epub 2007 Oct 15. PMID:18068379
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