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| | ==EBULIN COMPLEXED WITH LACTOSE, TRIGONAL CRYSTAL FORM== | | ==EBULIN COMPLEXED WITH LACTOSE, TRIGONAL CRYSTAL FORM== |
| - | <StructureSection load='1hwo' size='340' side='right' caption='[[1hwo]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='1hwo' size='340' side='right'caption='[[1hwo]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hwo]] 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=1HWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hwo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HWO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hwn|1hwn]], [[1hwm|1hwm]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1hwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwo OCA], [https://pdbe.org/1hwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hwo RCSB], [https://www.ebi.ac.uk/pdbsum/1hwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwo ProSAT]</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=1hwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwo OCA], [http://pdbe.org/1hwo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hwo RCSB], [http://www.ebi.ac.uk/pdbsum/1hwo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9AVR2_SAMEB Q9AVR2_SAMEB] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Sambucus ebulus]] | | [[Category: Sambucus ebulus]] |
| - | [[Category: RRNA N-glycosylase]]
| + | [[Category: Day PJ]] |
| - | [[Category: Day, P J]] | + | [[Category: Ernst SR]] |
| - | [[Category: Ernst, S R]] | + | [[Category: Monzingo AF]] |
| - | [[Category: Monzingo, A F]] | + | [[Category: Pascal JM]] |
| - | [[Category: Pascal, J M]] | + | [[Category: Robertus JD]] |
| - | [[Category: Robertus, J D]] | + | |
| - | [[Category: Galactoside lectin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ribosome-inactivating protein]]
| + | |
| - | [[Category: Ricin-like]]
| + | |
| Structural highlights
1hwo is a 2 chain structure with sequence from Sambucus ebulus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.9Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q9AVR2_SAMEB
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T. 2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l. Proteins. 2001 May 15;43(3):319-26. PMID:11288182
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