3ql2: Difference between revisions
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< | ==Crystal Structure of Ribonuclease A Variant A4C/D83E/V118C== | ||
<StructureSection load='3ql2' size='340' side='right'caption='[[3ql2]], [[Resolution|resolution]] 1.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ql2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QL2 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]] 1.49Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3ql2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ql2 OCA], [https://pdbe.org/3ql2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ql2 RCSB], [https://www.ebi.ac.uk/pdbsum/3ql2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ql2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Among the strategies that employ genetic engineering to stabilize proteins, the introduction of disulfide bonds has proven to be a very potential approach. As, however, the replacement of amino acid residues by cysteines and the subsequent formation of the covalent bond can result in a severe deformation of the parental protein structure, the stabilization effect is strongly context dependent. Alternatively, the introduction of charged amino acid residues at the surface, which may result in the formation of extra ionic interactions or hydrogen bonds, provide propitious means for protein stabilization. The generation of an extra disulfide bond between residues 4 and 118 in ribonuclease A had resulted in a stabilization by 6 degrees C or 7 kJ mol(-1) , which was mainly caused by a deceleration of the unfolding reaction [Pecher, P. & Arnold, U. (2009) Biophys Chem, 141, 21-28]. Here, Asp83 was replaced by Glu resulting in a comparable stabilization. Moreover, combination of both mutations led to an additive effect and the resulting ribonuclease A variant (T(m) approximately 76 degrees C, DeltaG degrees approximately 53 kJ mol(-1) ) is the most stable ribonuclease A variant described so far. The analysis of the crystal structure of A4C/D83E/V118C-ribonuclease A reveals the formation of a salt bridge between the gamma-carboxyl group of Glu83 and the epsilon-amino group of Lys104. Enzymes Ribonuclease (EC3.1.27.5) Structured digital abstract * RNase A and RNase A bind by x-ray crystallography (View interaction). | |||
Significant stabilization of ribonuclease A by additive effects.,Arnold U, Schopfel M FEBS J. 2012 May 17. doi: 10.1111/j.1742-4658.2012.08632.x. PMID:22594773<ref>PMID:22594773</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ql2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arnold | [[Category: Arnold U]] | ||
[[Category: Schoepfel | [[Category: Schoepfel M]] | ||
Latest revision as of 20:14, 1 November 2023
Crystal Structure of Ribonuclease A Variant A4C/D83E/V118CCrystal Structure of Ribonuclease A Variant A4C/D83E/V118C
Structural highlights
FunctionRNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] Publication Abstract from PubMedAmong the strategies that employ genetic engineering to stabilize proteins, the introduction of disulfide bonds has proven to be a very potential approach. As, however, the replacement of amino acid residues by cysteines and the subsequent formation of the covalent bond can result in a severe deformation of the parental protein structure, the stabilization effect is strongly context dependent. Alternatively, the introduction of charged amino acid residues at the surface, which may result in the formation of extra ionic interactions or hydrogen bonds, provide propitious means for protein stabilization. The generation of an extra disulfide bond between residues 4 and 118 in ribonuclease A had resulted in a stabilization by 6 degrees C or 7 kJ mol(-1) , which was mainly caused by a deceleration of the unfolding reaction [Pecher, P. & Arnold, U. (2009) Biophys Chem, 141, 21-28]. Here, Asp83 was replaced by Glu resulting in a comparable stabilization. Moreover, combination of both mutations led to an additive effect and the resulting ribonuclease A variant (T(m) approximately 76 degrees C, DeltaG degrees approximately 53 kJ mol(-1) ) is the most stable ribonuclease A variant described so far. The analysis of the crystal structure of A4C/D83E/V118C-ribonuclease A reveals the formation of a salt bridge between the gamma-carboxyl group of Glu83 and the epsilon-amino group of Lys104. Enzymes Ribonuclease (EC3.1.27.5) Structured digital abstract * RNase A and RNase A bind by x-ray crystallography (View interaction). Significant stabilization of ribonuclease A by additive effects.,Arnold U, Schopfel M FEBS J. 2012 May 17. doi: 10.1111/j.1742-4658.2012.08632.x. PMID:22594773[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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