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| | <StructureSection load='5gu4' size='340' side='right'caption='[[5gu4]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='5gu4' size='340' side='right'caption='[[5gu4]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gu4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GU4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GU4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gu4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GU4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.55Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gu4 OCA], [http://pdbe.org/5gu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gu4 RCSB], [http://www.ebi.ac.uk/pdbsum/5gu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gu4 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=5gu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gu4 OCA], [https://pdbe.org/5gu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gu4 RCSB], [https://www.ebi.ac.uk/pdbsum/5gu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gu4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO]] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity). | + | [https://www.uniprot.org/uniprot/RLA2_HUMAN RLA2_HUMAN] Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ricin|Ricin]] | + | *[[Ricin 3D structures|Ricin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Castor bean]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RRNA N-glycosylase]] | + | [[Category: Ricinus communis]] |
| - | [[Category: Shaw, P C]] | + | [[Category: Shaw PC]] |
| - | [[Category: Shi, W W]] | + | [[Category: Shi WW]] |
| - | [[Category: Sze, S Y]] | + | [[Category: Sze SY]] |
| - | [[Category: Tang, Y S]] | + | [[Category: Tang YS]] |
| - | [[Category: Wong, K B]] | + | [[Category: Wong KB]] |
| - | [[Category: Zhu, Z N]] | + | [[Category: Zhu ZN]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ribosomal p stalk protein]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ribosome-inactivating protein]]
| + | |
| - | [[Category: Ricin]]
| + | |
| Structural highlights
Function
RLA2_HUMAN Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478]
Publication Abstract from PubMed
Ricin is a type 2 ribosome-inactivating protein (RIP), containing a catalytic A chain and a lectin-like B chain. It inhibits protein synthesis by depurinating the N-glycosidic bond at alpha-sarcin/ricin loop (SRL) of the 28S rRNA, which thereby prevents the binding of elongation factors to the GTPase activation center of the ribosome. Here, we present the 1.6 A crystal structure of Ricin A chain (RTA) complexed to the C-terminal peptide of the ribosomal stalk protein P2, which plays a crucial role in specific recognition of elongation factors and recruitment of eukaryote-specific RIPs to the ribosomes. Our structure reveals that the C-terminal GFGLFD motif of P2 peptide is inserted into a hydrophobic pocket of RTA, while the interaction assays demonstrate the structurally untraced SDDDM motif of P2 peptide contributes to the interaction with RTA. This interaction mode of RTA and P protein is in contrast to that with trichosanthin (TCS), Shiga-toxin (Stx) and the active form of maize RIP (MOD), implying the flexibility of the P2 peptide-RIP interaction, for the latter to gain access to ribosome.
Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2.,Shi WW, Tang YS, Sze SY, Zhu ZN, Wong KB, Shaw PC Toxins (Basel). 2016 Oct 13;8(10). pii: E296. PMID:27754366[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shi WW, Tang YS, Sze SY, Zhu ZN, Wong KB, Shaw PC. Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2. Toxins (Basel). 2016 Oct 13;8(10). pii: E296. PMID:27754366 doi:http://dx.doi.org/10.3390/toxins8100296
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