1jl2
From Proteopedia
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
Overview
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.
About this Structure
1JL2 is a Single protein structure of sequence from Escherichia coli and thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Contributions of folding cores to the thermostabilities of two ribonucleases H., Robic S, Berger JM, Marqusee S, Protein Sci. 2002 Feb;11(2):381-9. PMID:11790848 Page seeded by OCA on Fri May 2 21:21:20 2008
