2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l.
Publication/Presentation Date
5-15-2001
Abstract
Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type-II RIP, ebulin is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. A normal level of ribosome-inactivating N-glycosidase activity, characteristic of the A chain of type-II RIP, has been demonstrated for ebulin l. However, ebulin is considered a nontoxic type-II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type-II RIP like ricin. The molecular cloning, amino acid sequence, and the crystal structure of ebulin l are presented and compared with ricin. Ebulin l is shown to bind an A-chain substrate analogue, pteroic acid, in the same manner as ricin. The galactoside-binding ability of ebulin l is demonstrated crystallographically with a complex of the B chain with galactose and with lactose. The negligible cytotoxicity of ebulin l is apparently due to a reduced affinity for galactosides. An altered mode of galactoside binding in the 2gamma subdomain of the lectin B chain primarily causes the reduced affinity.
Volume
43
Issue
3
First Page
319
Last Page
326
ISSN
0887-3585
Published In/Presented At
Pascal, J. M., Day, P. J., Monzingo, A. F., Ernst, S. R., Robertus, J. D., Iglesias, R., Pérez, Y., Férreras, J. M., Citores, L., & Girbés, T. (2001). 2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l. Proteins, 43(3), 319–326. https://doi.org/10.1002/prot.1043
Disciplines
Anesthesiology | Medicine and Health Sciences
PubMedID
11288182
Department(s)
Department of Anesthesiology
Document Type
Article