1JL2

Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H

1JL2 の概要

• エントリーDOI: 10.2210/pdb1jl2/pdb
• 分子名称: Chimera of Ribonuclease HI, Ribonuclease H (2 entities in total)
• 機能のキーワード: mixed alpha-beta protein, hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Cytoplasm : P0A7Y4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70403.83

構造登録者

Robic, S.,Berger, J.M.,Marqusee, S. (登録日: 2001-07-13, 公開日: 2002-01-18, 最終更新日: 2023-08-16)

主引用文献

Robic, S.,Berger, J.M.,Marqusee, S.
Contributions of folding cores to the thermostabilities of two ribonucleases H.
Protein Sci., 11:381-389, 2002

PubMed Abstract: To investigate the contribution of the folding cores to the thermodynamic stability of RNases H, we used rational design to create two chimeras composed of parts of a thermophilic and a mesophilic RNase H. Each chimera combines the folding core from one parent protein and the remaining parts of the other. Both chimeras form active, well-folded RNases H. Stability curves, based on CD-monitored chemical denaturations, show that the chimera with the thermophilic core is more stable, has a higher midpoint of thermal denaturation, and a lower change in heat capacity (DeltaCp) upon unfolding than the chimera with the mesophilic core. A possible explanation for the low DeltaCp of both the parent thermophilic RNase H and the chimera with the thermophilic core is the residual structure in the denatured state. On the basis of the studied parameters, the chimera with the thermophilic core resembles a true thermophilic protein. Our results suggest that the folding core plays an essential role in conferring thermodynamic parameters to RNases H.

PubMed: 11790848
DOI: 10.1110/ps.38602

実験手法

X-RAY DIFFRACTION (1.76 Å)