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| | <StructureSection load='6mv7' size='340' side='right'caption='[[6mv7]], [[Resolution|resolution]] 2.59Å' scene=''> | | <StructureSection load='6mv7' size='340' side='right'caption='[[6mv7]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mv7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MV7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MV7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MV7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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]] 2.59Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASE6, RNS6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6mv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mv7 OCA], [http://pdbe.org/6mv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mv7 RCSB], [http://www.ebi.ac.uk/pdbsum/6mv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mv7 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=6mv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mv7 OCA], [https://pdbe.org/6mv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mv7 RCSB], [https://www.ebi.ac.uk/pdbsum/6mv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mv7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RNAS6_HUMAN RNAS6_HUMAN]] May have a role in host defense. | + | [https://www.uniprot.org/uniprot/RNAS6_HUMAN RNAS6_HUMAN] May have a role in host defense. |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Couture, J F]] | + | [[Category: Couture J-F]] |
| - | [[Category: Doucet, N]] | + | [[Category: Doucet N]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nuclease]]
| + | |
| - | [[Category: Rnase]]
| + | |
| Structural highlights
Function
RNAS6_HUMAN May have a role in host defense.
Publication Abstract from PubMed
Ribonuclease 6 (RNase 6) is one of eight catalytically active human pancreatic-type RNases that belong to a superfamily of rapidly evolving enzymes. Like some of its human homologues, RNase 6 exhibits host defense properties such as antiviral and antibacterial activities. Recently solved crystal structures of this enzyme in its nucleotide-free form show the conservation of the prototypical kidney-shaped fold preserved among vertebrate RNases, in addition to revealing the presence of a unique secondary active site. In this study, we determine the structural and conformational properties experienced by RNase 6 upon binding to substrate and product analogues. We present the first crystal structures of RNase 6 bound to a nucleotide ligand (adenosine 5'-monophosphate), in addition to RNase 6 bound to phosphate ions. While the enzyme preserves B2 subsite ligand preferences, our results show a lack of typical B2 subsite interactions normally observed in homologous ligand-bound RNases. A comparison of the dynamical properties of RNase 6 in its apo-, substrate-, and product-bound states highlight the unique dynamical properties experienced on time scales ranging from nano- to milliseconds. Overall, our results confirm the specific evolutionary adaptation of RNase 6 relative to its unique catalytic and biological activities.
Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding.,Narayanan C, Bernard DN, Letourneau M, Gagnon J, Gagne D, Bafna K, Calmettes C, Couture JF, Agarwal PK, Doucet N Biochemistry. 2020 Feb 18;59(6):755-765. doi: 10.1021/acs.biochem.9b00888. Epub, 2020 Jan 24. PMID:31909602[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Narayanan C, Bernard DN, Letourneau M, Gagnon J, Gagne D, Bafna K, Calmettes C, Couture JF, Agarwal PK, Doucet N. Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding. Biochemistry. 2020 Feb 18;59(6):755-765. doi: 10.1021/acs.biochem.9b00888. Epub, 2020 Jan 24. PMID:31909602 doi:http://dx.doi.org/10.1021/acs.biochem.9b00888
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