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| <StructureSection load='3rh1' size='340' side='right'caption='[[3rh1]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3rh1' size='340' side='right'caption='[[3rh1]], [[Resolution|resolution]] 2.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3rh1]] 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=3RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rh1]] 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=3RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RH1 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.1Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kf2|1kf2]], [[1kf3|1kf3]], [[1kf5|1kf5]], [[1kf7|1kf7]], [[1fs3|1fs3]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rh1 OCA], [https://pdbe.org/3rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/3rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rh1 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=3rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rh1 OCA], [https://pdbe.org/3rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/3rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rh1 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: Balsamo A]] |
- | [[Category: Balsamo, A]] | + | [[Category: Mazzarella L]] |
- | [[Category: Mazzarella, L]] | + | [[Category: Merlino A]] |
- | [[Category: Merlino, A]] | + | [[Category: Sica F]] |
- | [[Category: Sica, F]] | + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Protei]]
| + | |
- | [[Category: Ribonuclease]]
| + | |
- | [[Category: Ribonuclease fold]]
| + | |
- | [[Category: Rna]]
| + | |
| 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
3D domain swapping is the process by which two or more protein molecules exchange part of their structure to form intertwined dimers or higher oligomers. Bovine pancreatic ribonuclease (RNase A) is able to swap the N-terminal alpha-helix (residues 1-13) and/or the C-terminal beta-strand (residues 116-124), thus forming a variety of oligomers, including two different dimers. Cis-trans isomerization of the Asn113-Pro114 peptide group was observed when the protein formed the C-terminal swapped dimer. To study the effect of the substitution of Pro114 on the swapping process of RNase A, we have prepared and characterized the P114A monomeric and dimeric variants of the enzyme. In contrast with previous reports, the crystal structure and NMR data on the monomer reveals a mixed cis-trans conformation for the Asn113-Ala114 peptide group, whereas the X-ray structure of the C-terminal swapped dimer of the variant is very close to that of the corresponding dimer of RNase A. The mutation at the C-terminus affects the capability of the N-terminal alpha-helix to swap and the stability of both dimeric forms. The present results underscore the importance of the hydration shell in determining the cross-talk between the chain termini in the swapping process of RNase A.
Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease.,Merlino A, Picone D, Ercole C, Balsamo A, Sica F Biochimie. 2012 Jan 17. PMID:22273774[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
- ↑ Merlino A, Picone D, Ercole C, Balsamo A, Sica F. Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease. Biochimie. 2012 Jan 17. PMID:22273774 doi:10.1016/j.biochi.2012.01.010
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