1qdo
From Proteopedia
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- | [[Image:1qdo.jpg|left|200px]] | + | [[Image:1qdo.jpg|left|200px]] |
- | + | ||
- | '''MAN(APLHA1-3)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX''' | + | {{Structure |
+ | |PDB= 1qdo |SIZE=350|CAPTION= <scene name='initialview01'>1qdo</scene>, resolution 2.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''MAN(APLHA1-3)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1QDO is a [ | + | 1QDO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDO OCA]. |
==Reference== | ==Reference== | ||
- | The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-6)Man(alpha1-O)Me in complex with concanavalin A., Bouckaert J, Hamelryck TW, Wyns L, Loris R, J Biol Chem. 1999 Oct 8;274(41):29188-95. PMID:[http:// | + | The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-6)Man(alpha1-O)Me in complex with concanavalin A., Bouckaert J, Hamelryck TW, Wyns L, Loris R, J Biol Chem. 1999 Oct 8;274(41):29188-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10506175 10506175] |
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: MN]] | [[Category: MN]] | ||
[[Category: carbohydrate binding]] | [[Category: carbohydrate binding]] | ||
- | [[Category: concanavalin | + | [[Category: concanavalin some]] |
[[Category: dimannose]] | [[Category: dimannose]] | ||
[[Category: plant lectin]] | [[Category: plant lectin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:15 2008'' |
Revision as of 11:36, 20 March 2008
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, resolution 2.8Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
MAN(APLHA1-3)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX
Overview
The crystal structures of concanavalin A in complex with Man(alpha1-6)Man(alpha1-O)Me and Man(alpha1-3)Man(alpha1-O)Me were determined at resolutions of 2.0 and 2.8 A, respectively. In both structures, the O-1-linked mannose binds in the conserved monosaccharide-binding site. The O-3-linked mannose of Man(alpha1-3)Man(alpha1-O)Me binds in the hydrophobic subsite formed by Tyr-12, Tyr-100, and Leu-99. The shielding of a hydrophobic surface is consistent with the associated large heat capacity change. The O-6-linked mannose of Man(alpha1-6)Man(alpha1-O)Me binds in the same subsite formed by Tyr-12 and Asp-16 as the reducing mannose of the highly specific trimannose Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me. However, it is much less tightly bound. Its O-2 hydroxyl makes no hydrogen bond with the conserved water 1. Water 1 is present in all the sugar-containing concanavalin A structures and increases the complementarity between the protein-binding surface and the sugar, but is not necessarily a hydrogen-bonding partner. A water analysis of the carbohydrate-binding site revealed a conserved water molecule replacing O-4 on the alpha1-3-linked arm of the trimannose. No such water is found for the reducing or O-6-linked mannose. Our data indicate that the central mannose of Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me primarily functions as a hinge between the two outer subsites.
About this Structure
1QDO is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-6)Man(alpha1-O)Me in complex with concanavalin A., Bouckaert J, Hamelryck TW, Wyns L, Loris R, J Biol Chem. 1999 Oct 8;274(41):29188-95. PMID:10506175
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