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| | ==Solution Structure of Cytotoxic RC-RNase4== | | ==Solution Structure of Cytotoxic RC-RNase4== |
| - | <StructureSection load='1kvz' size='340' side='right' caption='[[1kvz]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1kvz' size='340' side='right'caption='[[1kvz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kvz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/American_bullfrog American bullfrog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KVZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kvz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KVZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Oocytes ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8400 American bullfrog])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr> |
| - | <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=1kvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kvz OCA], [http://pdbe.org/1kvz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kvz RCSB], [http://www.ebi.ac.uk/pdbsum/1kvz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kvz 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=1kvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kvz OCA], [https://pdbe.org/1kvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kvz RCSB], [https://www.ebi.ac.uk/pdbsum/1kvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kvz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9DFY6_AQUCT Q9DFY6_AQUCT] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kv/1kvz_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kv/1kvz_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | ==See Also== | | ==See Also== |
| - | *[[Temp|Temp]] | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: American bullfrog]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, C]] | + | [[Category: Lithobates catesbeianus]] |
| - | [[Category: Chen, L W]] | + | [[Category: Chen C]] |
| - | [[Category: Hsu, C H]] | + | [[Category: Chen L-W]] |
| - | [[Category: Liao, Y D]] | + | [[Category: Hsu C-H]] |
| - | [[Category: Wu, S H]] | + | [[Category: Liao Y-D]] |
| - | [[Category: Antitumor]]
| + | [[Category: Wu S-H]] |
| - | [[Category: Bullfrog]]
| + | |
| - | [[Category: Cytotoxicity]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ribonuclease]]
| + | |
| - | [[Category: Structure from molmol]]
| + | |
| Structural highlights
Function
Q9DFY6_AQUCT
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytotoxic ribonucleases with antitumor activity are mainly found in the oocytes and early embryos of frogs. Native RC-RNase 4 (RNase 4), consisting of 106 residues linked with four disulfide bridges, is a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana. RNase 4 belongs to the bovine pancreatic ribonuclease (RNase A) superfamily. Recombinant RC-RNase 4 (rRNase 4), which contains an additional Met residue and glutamine instead of pyroglutamate at the N terminus, was found to possess less catalytic and cytotoxic activities than RNase 4. Equilibrium thermal and guanidine-HCl denaturation CD measurements revealed that RNase 4 is more thermally and chemically stable than rRNase 4. However, CD and NMR data showed that there is no gross conformational change between native and recombinant RNase 4. The NMR solution structure of rRNase 4 was determined to comprise three alpha-helices and two sets of antiparallel beta-sheets. Superimposition of each structure with the mean structure yielded an average root mean square deviation (RMSD) of 0.72(+/-0.14)A for the backbone atoms, and 1.42(+/-0.19)A for the heavy atoms in residues 3-105. A comparison of the 3D structure of rRNase 4 with the structurally and functionally related cytotoxic ribonuclease, onconase (ONC), showed that the two H-bonds in the N-terminal pyroglutamate of ONC were not present at the corresponding glutamine residue of rRNase 4. We suggest that the loss of these two H-bonds is one of the key factors responsible for the reductions of the conformational stability, catalytic and cytotoxic activities in rRNase 4. Furthermore, the differences of side-chain conformations of subsite residues among RNase A, ONC and rRNase 4 are related to their distinct catalytic activities and base preferences.
Solution structure of the cytotoxic RNase 4 from oocytes of bullfrog Rana catesbeiana.,Hsu CH, Liao YD, Pan YR, Chen LW, Wu SH, Leu YJ, Chen C J Mol Biol. 2003 Feb 28;326(4):1189-201. PMID:12589762[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hsu CH, Liao YD, Pan YR, Chen LW, Wu SH, Leu YJ, Chen C. Solution structure of the cytotoxic RNase 4 from oocytes of bullfrog Rana catesbeiana. J Mol Biol. 2003 Feb 28;326(4):1189-201. PMID:12589762
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