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3aly

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Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion

Structural highlights

3aly is a 2 chain structure with sequence from Sulfurisphaera tokodaii str. 7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.66Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3aly"

Categories: Large Structures | Sulfurisphaera tokodaii str. 7 | Angkawidjaja C | Kanaya S | Takano K

@@ Line 1: / Line 1: @@
 ==Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion==
-<StructureSection load='3aly' size='340' side='right' caption='[[3aly]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+<StructureSection load='3aly' size='340' side='right'caption='[[3aly]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3aly]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. 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]] 1.66&#8491;</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=273063 SULTO])</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>
-<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://pdbe.org/3aly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aly RCSB], [http://www.ebi.ac.uk/pdbsum/3aly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aly ProSAT]</span></td></tr>
 </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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ribonuclease H]]
+[[Category: Large Structures]]
-[[Category: Sulto]]
+[[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]]
-[[Category: Hydrolase]]
-[[Category: Thermostable rnase hi]]

3aly

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Current revision

Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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