View source for 3u01


==Crystal structure of onconase double mutant C30A/C75A at 1.12 A resolution==
<StructureSection load='3u01' size='340' side='right'caption='[[3u01]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3u01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_pipiens Lithobates pipiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U01 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]] 1.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3u01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u01 OCA], [https://pdbe.org/3u01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u01 RCSB], [https://www.ebi.ac.uk/pdbsum/3u01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u01 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNP30_LITPI RNP30_LITPI] Basic protein with antiproliferative/cytotoxic activity against several tumor cell lines in vitro, as well as antitumor in vivo. It exhibits a ribonuclease-like activity against high molecular weight ribosomal RNA.
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== Publication Abstract from PubMed ==
The structure of onconase C30A/C75A double mutant has been determined at 1.12A resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 454-460, 2014.

Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution.,Kurpiewska K, Torrent G, Ribo M, Loch JI, Vilanova M, Lewinski K Biopolymers. 2014 May;101(5):454-60. doi: 10.1002/bip.22403. PMID:23996687<ref>PMID:23996687</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u01" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lithobates pipiens]]
[[Category: Kurpiewska K]]
[[Category: Lewinski K]]
[[Category: Loch J]]
[[Category: Ribo M]]
[[Category: Torrent G]]
[[Category: Vilanova M]]