3his
From Proteopedia
(Difference between revisions)
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<StructureSection load='3his' size='340' side='right'caption='[[3his]], [[Resolution|resolution]] 1.49Å' scene=''> | <StructureSection load='3his' size='340' side='right'caption='[[3his]], [[Resolution|resolution]] 1.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3his]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3his]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saponaria_officinalis Saponaria officinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HIS FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49Å</td></tr> |
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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=3his FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3his OCA], [https://pdbe.org/3his PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3his RCSB], [https://www.ebi.ac.uk/pdbsum/3his PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3his ProSAT]</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=3his FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3his OCA], [https://pdbe.org/3his PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3his RCSB], [https://www.ebi.ac.uk/pdbsum/3his PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3his ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q2QEH4_SAPOF Q2QEH4_SAPOF] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=3his ConSurf]. | </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=3his ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Ricin A-chain (RTA) and saporin-L1 (SAP) catalyze adenosine depurination of 28S rRNA to inhibit protein synthesis and cause cell death. We present the crystal structures of RTA and SAP in complex with transition state analogue inhibitors. These tight-binding inhibitors mimic the sarcin-ricin recognition loop of 28S rRNA and the dissociative ribocation transition state established for RTA catalysis. RTA and SAP share unique purine-binding geometry with quadruple pi-stacking interactions between adjacent adenine and guanine bases and 2 conserved tyrosines. An arginine at one end of the pi-stack provides cationic polarization and enhanced leaving group ability to the susceptible adenine. Common features of these ribosome-inactivating proteins include adenine leaving group activation, a remarkable lack of ribocation stabilization, and conserved glutamates as general bases for activation of the H(2)O nucleophile. Catalytic forces originate primarily from leaving group activation evident in both RTA and SAP in complex with transition state analogues. | ||
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| - | Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins.,Ho MC, Sturm MB, Almo SC, Schramm VL Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20276-81. Epub 2009 Nov 17. PMID:19920175<ref>PMID:19920175</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3his" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Common soapwort]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saponaria officinalis]] |
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Ho | + | [[Category: Ho M]] |
| - | [[Category: Schramm | + | [[Category: Schramm VL]] |
| - | [[Category: Sturm | + | [[Category: Sturm MB]] |
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Current revision
Crystal structure of Saporin-L1 from Saponaria officinalis
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