2vs6: Difference between revisions
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<StructureSection load='2vs6' size='340' side='right'caption='[[2vs6]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2vs6' size='340' side='right'caption='[[2vs6]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VS6 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2vs6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VS6 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mrk|1mrk]], [[1giu|1giu]], [[1mrj|1mrj]], [[2jdl|2jdl]], [[1tcs|1tcs]], [[1gis|1gis]], [[1nli|1nli]], [[1j4g|1j4g]], [[1qd2|1qd2]], [[2jjr|2jjr]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mrk|1mrk]], [[1giu|1giu]], [[1mrj|1mrj]], [[2jdl|2jdl]], [[1tcs|1tcs]], [[1gis|1gis]], [[1nli|1nli]], [[1j4g|1j4g]], [[1qd2|1qd2]], [[2jjr|2jjr]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vs6 OCA], [https://pdbe.org/2vs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vs6 RCSB], [https://www.ebi.ac.uk/pdbsum/2vs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vs6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2vs6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2vs6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribosome inactivating protein|Ribosome inactivating protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:48, 7 July 2021
K173A, R174A, K177A-trichosanthinK173A, R174A, K177A-trichosanthin
Structural highlights
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 PubMedRibosome-inactivating proteins (RIPs) inhibit protein synthesis by enzymatically depurinating a specific adenine residue at the sarcin-ricin loop of the 28S rRNA, which thereby prevents the binding of elongation factors to the GTPase activation centre of the ribosome. Here, we present the 2.2 A crystal structure of trichosanthin (TCS) complexed to the peptide SDDDMGFGLFD, which corresponds to the conserved C-terminal elongation factor binding domain of the ribosomal P protein. The N-terminal region of this peptide interacts with Lys173, Arg174 and Lys177 in TCS, while the C-terminal region is inserted into a hydrophobic pocket. The interaction with the P protein contributes to the ribosome-inactivating activity of TCS. This 11-mer C-terminal P peptide can be docked with selected important plant and bacterial RIPs, indicating that a similar interaction may also occur with other RIPs. The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome.,Too PH, Ma MK, Mak AN, Wong YT, Tung CK, Zhu G, Au SW, Wong KB, Shaw PC Nucleic Acids Res. 2009 Feb;37(2):602-10. Epub 2008 Dec 10. PMID:19073700[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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