1ulm
From Proteopedia
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|PDB= 1ulm |SIZE=350|CAPTION= <scene name='initialview01'>1ulm</scene>, resolution 1.80Å | |PDB= 1ulm |SIZE=350|CAPTION= <scene name='initialview01'>1ulm</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ulk|1ULK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ulm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulm OCA], [http://www.ebi.ac.uk/pdbsum/1ulm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ulm RCSB]</span> | ||
}} | }} | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''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 00:11:57 2008'' |
Revision as of 21:12, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Related: | 1ULK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose
Overview
The roots of pokeweed (Phytolacca americana) are known to contain the lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A resolution. The polypeptide chains of PL-C and PL-D2 form three and two repetitive chitin-binding domains, respectively. In the crystal structure of the PL-D2 complex, one trisaccharide molecule is shared mainly between two neighboring molecules related to each other by a crystallographic 2(1)-screw axis, and infinite helical chains of complexed molecules are generated by the sharing of ligand molecules. The crystal structure of PL-C reveals that the molecule is a dimer of two identical subunits, whose polypeptide chains are located in a head-to-tail fashion by a molecular 2-fold axis. Three putative carbohydrate-binding sites in each subunit are located in the dimer interface. The dimerization of PL-C is performed through the hydrophobic interactions between the carbohydrate-binding sites of the opposite domains in the dimer, leading to a distinct dimerization mode from that of wheat-germ agglutinin. Three aromatic residues in each carbohydrate-binding site of PL-C are involved in the dimerization. These residues correspond to the residues that interact mainly with the trisaccharide in the PL-D2 complex and appear to mimic the saccharide residues in the complex. Consequently, the present structure of the PL-C dimer has no room for accommodating carbohydrate. The quaternary structure of PL-C formed through these putative carbohydrate-binding residues may lead to the lack of hemagglutinating activity.
About this Structure
1ULM is a Protein complex structure of sequences from Phytolacca americana. Full crystallographic information is available from OCA.
Reference
Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed., Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y, J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194
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