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| | ==A TRICHOSANTHIN(TCS) MUTANT(E85R) COMPLEX STRUCTURE WITH ADENINE== | | ==A TRICHOSANTHIN(TCS) MUTANT(E85R) COMPLEX STRUCTURE WITH ADENINE== |
| - | <StructureSection load='1giu' size='340' side='right' caption='[[1giu]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1giu' size='340' side='right'caption='[[1giu]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1giu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_cucumber Chinese cucumber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GIU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1giu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GIU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gis|1gis]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</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=1giu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1giu OCA], [https://pdbe.org/1giu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1giu RCSB], [https://www.ebi.ac.uk/pdbsum/1giu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1giu 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=1giu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1giu OCA], [http://pdbe.org/1giu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1giu RCSB], [http://www.ebi.ac.uk/pdbsum/1giu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1giu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RIPT_TRIKI RIPT_TRIKI]] Inactivates eukaryotic 60S ribosomal subunits. | + | [https://www.uniprot.org/uniprot/RIPT_TRIKI RIPT_TRIKI] Inactivates eukaryotic 60S ribosomal subunits. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1giu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1giu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chinese cucumber]] | + | [[Category: Large Structures]] |
| - | [[Category: RRNA N-glycosylase]] | + | [[Category: Trichosanthes kirilowii]] |
| - | [[Category: Dong, Y]] | + | [[Category: Dong Y]] |
| - | [[Category: Guo, Q]] | + | [[Category: Guo Q]] |
| - | [[Category: Liu, Y]] | + | [[Category: Liu Y]] |
| - | [[Category: Rao, Z]] | + | [[Category: Rao Z]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protein-sub complex]]
| + | |
| - | [[Category: Tc]]
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| - | [[Category: Trichosanthin]]
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| Structural highlights
Function
RIPT_TRIKI Inactivates eukaryotic 60S ribosomal subunits.
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
Trichosanthin (TCS) is a type I ribosome-inactivating protein (RIP) which possesses rRNA N-glycosidase activity. In recent years, its immunomodulatory, anti-tumor and anti-HIV properties have been revealed. Here we report the crystal structures of several E85 mutant TCS complexes with adenosine-5'-monophosphate (AMP) and adenine. In E85Q TCS/AMP and E85A TCS/AMP, near the active site of the molecule and parallel to the aromatic ring of Tyr70, an AMP molecule is bound to the mutant without being hydrolyzed. In the E85R TCS/adenine complex, the hydrolyzed product adenine is located in the active pocket where it occupies a position similar to that in the TCS/NADPH complex. Significantly, AMP is bound in a position different to that of adenine. In comparison with these structures, we suggest that there are at least two subsites in the active site of TCS, one for initial substrate recognition as revealed by the AMP site and another for catalysis as represented by the NADPH site. Based on these complex structures, the function of residue 85 and the mechanism of catalysis are proposed.
Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants.,Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z Protein Eng. 2003 Jun;16(6):391-6. PMID:12874371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guo Q, Zhou W, Too HM, Li J, Liu Y, Bartlam M, Dong Y, Wong KB, Shaw PC, Rao Z. Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants. Protein Eng. 2003 Jun;16(6):391-6. PMID:12874371
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