1hwn

<table><tr><td colspan='2'>[[1hwn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hwm|1hwm]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwn OCA], [http://pdbe.org/1hwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hwn RCSB], [http://www.ebi.ac.uk/pdbsum/1hwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwn ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11288182</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hwn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Day, P J]]

[[Category: Ernst, S R]]

[[Category: Monzingo, A F]]

[[Category: Pascal, J M]]

[[Category: Robertus, J D]]

[[Category: Ricin-like]]