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| | <StructureSection load='3ql1' size='340' side='right'caption='[[3ql1]], [[Resolution|resolution]] 1.29Å' scene=''> | | <StructureSection load='3ql1' size='340' side='right'caption='[[3ql1]], [[Resolution|resolution]] 1.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ql1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QL1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ql1]] is a 1 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=3QL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QL1 FirstGlance]. <br> |
| - | </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.29Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ql2|3ql2]]</div></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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASE1, RNS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </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=3ql1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ql1 OCA], [https://pdbe.org/3ql1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ql1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ql1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ql1 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=3ql1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ql1 OCA], [https://pdbe.org/3ql1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ql1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ql1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ql1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pancreatic ribonuclease]]
| + | [[Category: Arnold U]] |
| - | [[Category: Arnold, U]] | + | [[Category: Schoepfel M]] |
| - | [[Category: Schoepfel, M]] | + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Folding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Proteolysis]]
| + | |
| - | [[Category: Ribonuclease some]]
| + | |
| - | [[Category: Salt bridge]]
| + | |
| - | [[Category: Site-directed mutagenesis]]
| + | |
| - | [[Category: Stability]]
| + | |
| Structural highlights
Function
RNAS1_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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
- ↑ Arnold U, Schopfel M. Significant stabilization of ribonuclease A by additive effects. FEBS J. 2012 May 17. doi: 10.1111/j.1742-4658.2012.08632.x. PMID:22594773 doi:10.1111/j.1742-4658.2012.08632.x
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