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| | ==Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion== | | ==Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion== |
| - | <StructureSection load='3aly' size='340' side='right' caption='[[3aly]], [[Resolution|resolution]] 1.66Å' scene=''> | + | <StructureSection load='3aly' size='340' side='right'caption='[[3aly]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aly]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ALY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aly]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ALY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ehg|2ehg]]</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]] 1.66Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST0753 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=111955 Sulfolobus tokodaii])</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=3aly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aly OCA], [https://pdbe.org/3aly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aly RCSB], [https://www.ebi.ac.uk/pdbsum/3aly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aly ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </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=3aly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aly OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aly RCSB], [http://www.ebi.ac.uk/pdbsum/3aly PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RNH_SULTO RNH_SULTO] Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn(2+) or Co(2+) can also cleave an RNA-RNA hybrid; the dsRNase activity is 10- 100-fold lower than RNase H activity. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.<ref>PMID:15520465</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3aly" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ribonuclease H]] | + | [[Category: Large Structures]] |
| - | [[Category: Sulfolobus tokodaii]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Angkawidjaja, C]] | + | [[Category: Angkawidjaja C]] |
| - | [[Category: Kanaya, S]] | + | [[Category: Kanaya S]] |
| - | [[Category: Takano, K]] | + | [[Category: Takano K]] |
| - | [[Category: C-terminal anchor deletion]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Thermostable rnase hi]]
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| Structural highlights
Function
RNH_SULTO Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn(2+) or Co(2+) can also cleave an RNA-RNA hybrid; the dsRNase activity is 10- 100-fold lower than RNase H activity. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant.[1]
Publication Abstract from PubMed
RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, the stabilization effect of the Sto-RNase HI C-terminal residues was investigated in detail by thermodynamic measurements of the stability of variants lacking the disulfide bond (C58/145A), or the six C-terminal residues (DeltaC6) and by structural analysis of DeltaC6. The results showed that the C-terminal does not affect overall structure and stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a "stabilization tag." The Sto-RNase HI C-terminal residues (-IGCIILT) were introduced as a tag on three proteins. Each chimeric protein was more stable than its wild-type protein. These results suggested the possibility of a simple stabilization technique using a stabilization tag such as Sto-RNase HI C-terminal residues.
Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag.,Takano K, Okamoto T, Okada J, Tanaka S, Angkawidjaja C, Koga Y, Kanaya S PLoS One. 2011 Jan 19;6(1):e16226. PMID:21283826[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohtani N, Yanagawa H, Tomita M, Itaya M. Cleavage of double-stranded RNA by RNase HI from a thermoacidophilic archaeon, Sulfolobus tokodaii 7. Nucleic Acids Res. 2004 Nov 1;32(19):5809-19. PMID:15520465 doi:10.1093/nar/gkh917
- ↑ Takano K, Okamoto T, Okada J, Tanaka S, Angkawidjaja C, Koga Y, Kanaya S. Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag. PLoS One. 2011 Jan 19;6(1):e16226. PMID:21283826 doi:10.1371/journal.pone.0016226
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