1HWN

EBULIN COMPLEXED WITH GALACTOSE, TRIGONAL CRYSTAL FORM

Summary for 1HWN

• Entry DOI: 10.2210/pdb1hwn/pdb
• Related: 1HWM
• Descriptor: EBULIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose, ... (5 entities in total)
• Functional Keywords: ribosome-inactivating protein, ricin-like, galactoside lectin, hydrolase
• Biological source: Sambucus ebulus; More
• Total number of polymer chains: 2
• Total formula weight: 58641.59

Authors

Pascal, J.M.,Day, P.J.,Monzingo, A.F.,Ernst, S.R.,Robertus, J.D. (deposition date: 2001-01-09, release date: 2001-01-24, Last modification date: 2024-04-03)

Primary citation

Pascal, J.M.,Day, P.J.,Monzingo, A.F.,Ernst, S.R.,Robertus, J.D.,Iglesias, R.,Perez, Y.,Ferreras, J.M.,Citores, L.,Girbes, T.
2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l.
Proteins, 43:319-326, 2001

PubMed 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.

PubMed: 11288182
DOI: 10.1002/prot.1043

Experimental method

X-RAY DIFFRACTION (2.8 Å)