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3aly
From Proteopedia
(Difference between revisions)
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| - | + | ==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=''> | |
| - | + | == 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> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ehg|2ehg]]</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='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://www.rcsb.org/pdb/explore.do?structureId=3aly RCSB], [http://www.ebi.ac.uk/pdbsum/3aly PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21283826</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Sulfolobus tokodaii]] | [[Category: Sulfolobus tokodaii]] | ||
| - | [[Category: Angkawidjaja, C | + | [[Category: Angkawidjaja, C]] |
| - | [[Category: Kanaya, S | + | [[Category: Kanaya, S]] |
| - | [[Category: Takano, K | + | [[Category: Takano, K]] |
[[Category: C-terminal anchor deletion]] | [[Category: C-terminal anchor deletion]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Thermostable rnase hi]] | [[Category: Thermostable rnase hi]] | ||
Revision as of 13:52, 18 December 2014
Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion
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