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
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OverviewOverview
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 StructureAbout this Structure
1JL2 is a Single protein structure of sequence from Escherichia coli and thermus thermophilus. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.
ReferenceReference
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
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