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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ctk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bougainvillea_spectabilis Bougainvillea spectabilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wuc 1wuc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CTK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ctk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bougainvillea_spectabilis Bougainvillea spectabilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wuc 1wuc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CTK FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=3ctk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctk OCA], [https://pdbe.org/3ctk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ctk RCSB], [https://www.ebi.ac.uk/pdbsum/3ctk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ctk 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=3ctk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctk OCA], [https://pdbe.org/3ctk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ctk RCSB], [https://www.ebi.ac.uk/pdbsum/3ctk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ctk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8W4U4_9CARY Q8W4U4_9CARY]
== 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=3ctk 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=3ctk ConSurf].
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== Publication Abstract from PubMed ==
The three-dimensional structures of two type 1 RIPs, bouganin and lychnin, has been solved. Their adenine polynucleotide glycosylase activity was also determined together with other known RIPs: dianthin 30, PAP-R, momordin I, ricin A chain and saporin-S6. Saporin-S6 releases the highest number of adenine molecules from rat ribosomes, and poly(A), while its efficiency is similar to dianthin 30, bouganin and PAP-R on herring sperm DNA. Measures of the protein synthesis inhibitory activity confirmed that saporin-S6 is the most active. The overall structure of bouganin and lychnin is similar to the other considered RIPs and the typical RIP fold is conserved. The superimpositioning of their C(alpha) atoms highlights some differences in the N-terminal and C-terminal domains. A detailed structural analysis indicates that the efficiency of saporin-S6 on various polynucleotides can be ascribed to a negative electrostatic surface potential at the active site and several exposed positively charged residues in the region around that site. These two conditions, not present at the same time in other examined RIPs, could guarantee an efficient interaction with the substrate and an efficient catalysis.
Structure/function studies on two type 1 ribosome inactivating proteins: Bouganin and lychnin.,Fermani S, Tosi G, Farini V, Polito L, Falini G, Ripamonti A, Barbieri L, Chambery A, Bolognesi A J Struct Biol. 2009 Nov;168(2):278-87. Epub 2009 Jul 16. PMID:19616098<ref>PMID:19616098</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ctk" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosome inactivating protein|Ribosome inactivating protein]]
*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bougainvillea spectabilis]]
[[Category: Bougainvillea spectabilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RRNA N-glycosylase]]
[[Category: Bolognesi A]]
[[Category: Bolognesi, A]]
[[Category: Falini G]]
[[Category: Falini, G]]
[[Category: Farini V]]
[[Category: Farini, V]]
[[Category: Fermani S]]
[[Category: Fermani, S]]
[[Category: Polito L]]
[[Category: Polito, L]]
[[Category: Ripamonti A]]
[[Category: Ripamonti, A]]
[[Category: Tosi G]]
[[Category: Tosi, G]]
[[Category: Alpha-beta protein]]
[[Category: Hydrolase]]

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