1fat
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed, lectin from Phaseolus vulgaris, has been solved with molecular replacement, using the coordinates of lentil lectin as model, and refined at a, resolution of 2.8 A. The final R-factor of the structure is 20.0%. The, quaternary structure of the PHA-L tetramer differs from the structures of, the concanavalin A and peanut lectin tetramers, but resembles the, structure of the soybean agglutinin tetramer. PHA-L consists of two, canonical legume lectin dimers that pack together through the formation of, a close contact between two beta-strands. Of the two covalently bound, oligosaccharides per monomer, only one GlcNAc residue per monomer is, visible in the electron density. In this article we describe the structure, of .. | + | The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed, lectin from Phaseolus vulgaris, has been solved with molecular replacement, using the coordinates of lentil lectin as model, and refined at a, resolution of 2.8 A. The final R-factor of the structure is 20.0%. The, quaternary structure of the PHA-L tetramer differs from the structures of, the concanavalin A and peanut lectin tetramers, but resembles the, structure of the soybean agglutinin tetramer. PHA-L consists of two, canonical legume lectin dimers that pack together through the formation of, a close contact between two beta-strands. Of the two covalently bound, oligosaccharides per monomer, only one GlcNAc residue per monomer is, visible in the electron density. In this article we describe the structure, of PHA-L, and we discuss the putative position of the high affinity, adenine-binding site present in a number of legume lectins. A comparison, with transthyretin, a protein that shows a remarkable resemblance to, PHA-L, gives further ground to our proposal. |
==About this Structure== | ==About this Structure== | ||
| - | 1FAT is a | + | 1FAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] with NAG, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: CAA, CAB, CAC, CAD, MNA, MNB, MNC and MND. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: plant defense protein]] | [[Category: plant defense protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:41:19 2007'' |
Revision as of 11:36, 5 November 2007
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PHYTOHEMAGGLUTININ-L
Overview
The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed, lectin from Phaseolus vulgaris, has been solved with molecular replacement, using the coordinates of lentil lectin as model, and refined at a, resolution of 2.8 A. The final R-factor of the structure is 20.0%. The, quaternary structure of the PHA-L tetramer differs from the structures of, the concanavalin A and peanut lectin tetramers, but resembles the, structure of the soybean agglutinin tetramer. PHA-L consists of two, canonical legume lectin dimers that pack together through the formation of, a close contact between two beta-strands. Of the two covalently bound, oligosaccharides per monomer, only one GlcNAc residue per monomer is, visible in the electron density. In this article we describe the structure, of PHA-L, and we discuss the putative position of the high affinity, adenine-binding site present in a number of legume lectins. A comparison, with transthyretin, a protein that shows a remarkable resemblance to, PHA-L, gives further ground to our proposal.
About this Structure
1FAT is a Single protein structure of sequence from Phaseolus vulgaris with NAG, MN and CA as ligands. Structure known Active Sites: CAA, CAB, CAC, CAD, MNA, MNB, MNC and MND. Full crystallographic information is available from OCA.
Reference
The crystallographic structure of phytohemagglutinin-L., Hamelryck TW, Dao-Thi MH, Poortmans F, Chrispeels MJ, Wyns L, Loris R, J Biol Chem. 1996 Aug 23;271(34):20479-85. PMID:8702788
Page seeded by OCA on Mon Nov 5 13:41:19 2007
Categories: Phaseolus vulgaris | Single protein | Hamelryck, T. | Loris, R. | CA | MN | NAG | Glycoprotein | Lectin | Plant defense protein
