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1hwp
From Proteopedia
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(New page: 200px<br /><applet load="1hwp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hwp, resolution 3.1Å" /> '''EBULIN COMPLEXED WITH...)
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Revision as of 01:03, 25 November 2007
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EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM
Overview
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.
About this Structure
1HWP is a Protein complex structure of sequences from Sambucus ebulus with PT1 as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l., Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T, Proteins. 2001 May 15;43(3):319-26. PMID:11288182
Page seeded by OCA on Sun Nov 25 03:11:15 2007
