1FAT
PHYTOHEMAGGLUTININ-L
Summary for 1FAT
| Entry DOI | 10.2210/pdb1fat/pdb |
| Descriptor | PHYTOHEMAGGLUTININ-L, 2-acetamido-2-deoxy-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | glycoprotein, plant defense protein, lectin |
| Biological source | Phaseolus vulgaris |
| Total number of polymer chains | 4 |
| Total formula weight | 111017.94 |
| Authors | Hamelryck, T.,Loris, R. (deposition date: 1996-06-12, release date: 1996-12-23, Last modification date: 2024-10-23) |
| Primary citation | Hamelryck, T.W.,Dao-Thi, M.H.,Poortmans, F.,Chrispeels, M.J.,Wyns, L.,Loris, R. The crystallographic structure of phytohemagglutinin-L. J.Biol.Chem., 271:20479-20485, 1996 Cited by PubMed Abstract: 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. PubMed: 8702788DOI: 10.1074/jbc.271.34.20479 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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