Abstract
The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5398-5403 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 262 |
| Issue number | 11 |
| State | Published - Apr 15 1987 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Cite this
Montfort, W., Villafranca, J. E., Monzingo, A. F., Ernst, S. R., Katzin, B., Rutenber, E., Xuong, N. H., Hamlin, R., & Robertus, J. D. (1987). The three-dimensional structure of ricin at 2.8 A. Journal of Biological Chemistry, 262(11), 5398-5403.