Title | The crystallographic structure of phytohemagglutinin-L. |
Publication Type | Journal Article |
Year of Publication | 1996 |
Authors | Hamelryck, T. W., M-H. Dao-Thi, F. Poortmans, M. J. Chrispeels, L. Wyns, and R. Loris |
Journal | J Biol Chem |
Volume | 271 |
Issue | 34 |
Pagination | 20479-85 |
Date Published | 1996 Aug 23 |
ISSN | 0021-9258 |
Keywords | Binding Sites, Concanavalin A, Crystallography, X-Ray, Models, Molecular, Phytohemagglutinins, Plant Proteins, Prealbumin, Protein Conformation |
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. |
Alternate Journal | J. Biol. Chem. |
PubMed ID | 8702788 |
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