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1zgs
From Proteopedia
(New page: 200px<br /><applet load="1zgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zgs, resolution 2.50Å" /> '''Parkia platycephala ...) |
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| - | [[Image:1zgs.gif|left|200px]]<br /><applet load="1zgs" size=" | + | [[Image:1zgs.gif|left|200px]]<br /><applet load="1zgs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zgs, resolution 2.50Å" /> | caption="1zgs, resolution 2.50Å" /> | ||
'''Parkia platycephala seed lectin in complex with 5-bromo-4-chloro-3-indolyl-a-D-mannose'''<br /> | '''Parkia platycephala seed lectin in complex with 5-bromo-4-chloro-3-indolyl-a-D-mannose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of the apo and mannose-bound Parkia platycephala | + | The crystal structures of the apo and mannose-bound Parkia platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of beta-prism domains, and highlight the adaptability of the beta-prism fold as a building block in the evolution of plant lectins. The P.platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P.platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P.platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala] with XMM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala] with <scene name='pdbligand=XMM:'>XMM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Parkia platycephala]] | [[Category: Parkia platycephala]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Calvete, J | + | [[Category: Calvete, J J.]] |
| - | [[Category: Cavada, B | + | [[Category: Cavada, B S.]] |
| - | [[Category: Sol, F | + | [[Category: Sol, F Gallego del.]] |
[[Category: XMM]] | [[Category: XMM]] | ||
[[Category: beta prism]] | [[Category: beta prism]] | ||
| Line 21: | Line 21: | ||
[[Category: x-man]] | [[Category: x-man]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:23 2008'' |
Revision as of 14:15, 21 February 2008
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Parkia platycephala seed lectin in complex with 5-bromo-4-chloro-3-indolyl-a-D-mannose
Overview
The crystal structures of the apo and mannose-bound Parkia platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of beta-prism domains, and highlight the adaptability of the beta-prism fold as a building block in the evolution of plant lectins. The P.platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P.platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P.platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
About this Structure
1ZGS is a Single protein structure of sequence from Parkia platycephala with as ligand. Full crystallographic information is available from OCA.
Reference
The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain., Gallego del Sol F, Nagano C, Cavada BS, Calvete JJ, J Mol Biol. 2005 Oct 28;353(3):574-83. Epub 2005 Sep 9. PMID:16185708
Page seeded by OCA on Thu Feb 21 16:15:23 2008
