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< | ==Crystal Structure of the Ribotoxin Restrictocin and a 31-mer SRD RNA Inhibitor== | ||
<StructureSection load='1jbr' size='340' side='right'caption='[[1jbr]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jbr]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_restrictus Aspergillus restrictus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JBR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A23:ADENOSINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>A23</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=1jbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbr OCA], [https://pdbe.org/1jbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jbr RCSB], [https://www.ebi.ac.uk/pdbsum/1jbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jbr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNMG_ASPRE RNMG_ASPRE] This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/1jbr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1jbr ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cytotoxin sarcin disrupts elongation factor binding and protein synthesis by specifically cleaving one phosphodiester bond in ribosomes. To elucidate the molecular basis of toxin action, we determined three cocrystal structures of the sarcin homolog restrictocin bound to different analogs that mimic the target sarcin/ricin loop (SRL) structure of the rat 28S rRNA. In these structures, restrictocin contacts the bulged-G motif and an unfolded form of the tetraloop of the SRL RNA. In one structure, toxin loops guide selection of the target site by contacting the base critical for recognition (G4319) and the surrounding S-shaped backbone. In another structure, base flipping of the tetraloop enables cleavage by placing the target nucleotide in the active site with the nucleophile nearly inline for attack on the scissile bond. These structures provide the first views of how a site-specific protein endonuclease recognizes and cleaves a folded RNA substrate. | |||
Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping.,Yang X, Gerczei T, Glover LT, Correll CC Nat Struct Biol. 2001 Nov;8(11):968-73. PMID:11685244<ref>PMID:11685244</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1jbr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Aspergillus restrictus]] | [[Category: Aspergillus restrictus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Correll | [[Category: Correll CC]] | ||
[[Category: Gerczei | [[Category: Gerczei T]] | ||
[[Category: Glover | [[Category: Glover L]] | ||
[[Category: Yang | [[Category: Yang X]] | ||
Latest revision as of 07:38, 17 October 2024
Crystal Structure of the Ribotoxin Restrictocin and a 31-mer SRD RNA InhibitorCrystal Structure of the Ribotoxin Restrictocin and a 31-mer SRD RNA Inhibitor
Structural highlights
FunctionRNMG_ASPRE This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity. 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 PubMedThe cytotoxin sarcin disrupts elongation factor binding and protein synthesis by specifically cleaving one phosphodiester bond in ribosomes. To elucidate the molecular basis of toxin action, we determined three cocrystal structures of the sarcin homolog restrictocin bound to different analogs that mimic the target sarcin/ricin loop (SRL) structure of the rat 28S rRNA. In these structures, restrictocin contacts the bulged-G motif and an unfolded form of the tetraloop of the SRL RNA. In one structure, toxin loops guide selection of the target site by contacting the base critical for recognition (G4319) and the surrounding S-shaped backbone. In another structure, base flipping of the tetraloop enables cleavage by placing the target nucleotide in the active site with the nucleophile nearly inline for attack on the scissile bond. These structures provide the first views of how a site-specific protein endonuclease recognizes and cleaves a folded RNA substrate. Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping.,Yang X, Gerczei T, Glover LT, Correll CC Nat Struct Biol. 2001 Nov;8(11):968-73. PMID:11685244[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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