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| ==Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant== | | ==Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant== |
- | <StructureSection load='4n4c' size='340' side='right' caption='[[4n4c]], [[Resolution|resolution]] 2.48Å' scene=''> | + | <StructureSection load='4n4c' size='340' side='right'caption='[[4n4c]], [[Resolution|resolution]] 2.48Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4n4c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n4c]] 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=4N4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4C FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</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=4n4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4c OCA], [https://pdbe.org/4n4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4c RCSB], [https://www.ebi.ac.uk/pdbsum/4n4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4c ProSAT]</span></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f0v|1f0v]], [[3rid|3rid]], [[1n1x|1n1x]]</td></tr>
| + | |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRN ([http://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'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span></td></tr>
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4c OCA], [http://pdbe.org/4n4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n4c RCSB], [http://www.ebi.ac.uk/pdbsum/4n4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4c ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/RNS_BOVIN RNS_BOVIN]] This enzyme hydrolyzes both single- and double-stranded RNA. | + | [https://www.uniprot.org/uniprot/RNS_BOVIN RNS_BOVIN] This enzyme hydrolyzes both single- and double-stranded RNA. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
- | *[[Ribonuclease|Ribonuclease]] | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
- | *[[Temp|Temp]]
| + | |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
- | [[Category: Pancreatic ribonuclease]] | + | [[Category: Large Structures]] |
- | [[Category: Krauss, I Russo]]
| + | [[Category: Merlino A]] |
- | [[Category: Merlino, A]] | + | [[Category: Pica A]] |
- | [[Category: Pica, A]] | + | [[Category: Russo Krauss I]] |
- | [[Category: Sica, F]] | + | [[Category: Sica F]] |
- | [[Category: C-terminal domain swapping]] | + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Ribonuclease]]
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| Structural highlights
Function
RNS_BOVIN This enzyme hydrolyzes both single- and double-stranded RNA.
Publication Abstract from PubMed
Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed.
The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D. The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer. FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346 doi:http://dx.doi.org/10.1016/j.febslet.2013.10.003
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