View source for 6qmn


==Crystal structure of a Ribonuclease A-Onconase chimera==
<StructureSection load='6qmn' size='340' side='right'caption='[[6qmn]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qmn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bison_bison Bison bison]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QMN 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]] 2.31&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6qmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qmn OCA], [https://pdbe.org/6qmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qmn RCSB], [https://www.ebi.ac.uk/pdbsum/6qmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qmn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNAS1_BISBI RNAS1_BISBI] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural roles of loop regions are frequently overlooked in proteins. Nevertheless, they may be key players in the definition of protein topology and in the self-assembly processes occurring through domain swapping. We here investigate the effects on structure and stability of replacing the loop connecting the last two beta-strands of RNase A with the corresponding region of the more thermostable Onconase. The crystal structure of this chimeric variant (RNaseA-ONC) shows that its terminal loop size better adheres to the topological rules for the design of stabilized proteins, proposed by Baker and coworkers [43]. Indeed, RNaseA-ONC displays a thermal stability close to that of RNase A, despite the lack of Pro at position 114, which, due to its propensity to favor a cis peptide bond, has been identified as an important stabilizing factor of the native protein. Accordingly, RNaseA-ONC is significantly more stable than RNase A variants lacking Pro114; RNaseA-ONC also displays a higher propensity to form oligomers in native conditions when compared to either RNase A or Onconase. This finding demonstrates that modifications of terminal loops should to be carefully controlled in terms of size and sequence to avoid unwanted and/or potentially harmful aggregation processes.

Structure, stability and aggregation propensity of a Ribonuclease A-Onconase chimera.,Esposito L, Donnarumma F, Ruggiero A, Leone S, Vitagliano L, Picone D Int J Biol Macromol. 2019 Apr 23. pii: S0141-8130(19)31077-3. doi:, 10.1016/j.ijbiomac.2019.04.164. PMID:31026530<ref>PMID:31026530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6qmn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bison bison]]
[[Category: Large Structures]]
[[Category: Donnarumma F]]
[[Category: Esposito L]]
[[Category: Leone S]]
[[Category: Picone D]]
[[Category: Ruggiero A]]
[[Category: Vitagliano L]]