1hwm

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[[Image:1hwm.gif|left|200px]]
 
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{{Structure
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==EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL==
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|PDB= 1hwm |SIZE=350|CAPTION= <scene name='initialview01'>1hwm</scene>, resolution 2.8&Aring;
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<StructureSection load='1hwm' size='340' side='right'caption='[[1hwm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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<table><tr><td colspan='2'>[[1hwm]] 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=1HWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HWM FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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|GENE=
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<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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwm OCA], [https://pdbe.org/1hwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hwm RCSB], [https://www.ebi.ac.uk/pdbsum/1hwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwm ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwm OCA], [http://www.ebi.ac.uk/pdbsum/1hwm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hwm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q9AVR2_SAMEB Q9AVR2_SAMEB]
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== Evolutionary Conservation ==
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'''EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/1hwm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hwm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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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.
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.
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==About this Structure==
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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>
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1HWM is a [[Protein complex]] structure of sequences 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=1HWM OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11288182 11288182]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1hwm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Sambucus ebulus]]
[[Category: Sambucus ebulus]]
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[[Category: rRNA N-glycosylase]]
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[[Category: Day PJ]]
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[[Category: Day, P J.]]
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[[Category: Ernst SR]]
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[[Category: Ernst, S R.]]
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[[Category: Monzingo AF]]
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[[Category: Monzingo, A F.]]
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[[Category: Pascal JM]]
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[[Category: Pascal, J M.]]
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[[Category: Robertus JD]]
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[[Category: Robertus, J D.]]
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[[Category: ribosome-inactivating protein]]
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[[Category: ricin-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:20 2008''
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Current revision

EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL

PDB ID 1hwm

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