3ALY

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

Summary for 3ALY

• Entry DOI: 10.2210/pdb3aly/pdb
• Related: 2ehg
• Descriptor: Putative uncharacterized protein ST0753 (2 entities in total)
• Functional Keywords: thermostable rnase hi, c-terminal anchor deletion, hydrolase
• Biological source: Sulfolobus tokodaii
• Total number of polymer chains: 2
• Total formula weight: 32470.11

Authors

Angkawidjaja, C.,Takano, K.,Kanaya, S. (deposition date: 2010-08-10, release date: 2011-06-22, Last modification date: 2023-11-01)

Primary citation

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, 6:e16226-e16226, 2011

PubMed Abstract: 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 (ΔC6) and by structural analysis of ΔC6. 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.

PubMed: 21283826
DOI: 10.1371/journal.pone.0016226

Experimental method

X-RAY DIFFRACTION (1.66 Å)