1jl2: Difference between revisions
New page: left|200px<br /><applet load="1jl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jl2, resolution 1.76Å" /> '''Crystal structure of... |
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[[Image:1jl2.gif|left|200px]]<br /><applet load="1jl2" size=" | [[Image:1jl2.gif|left|200px]]<br /><applet load="1jl2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jl2, resolution 1.76Å" /> | caption="1jl2, resolution 1.76Å" /> | ||
'''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'''<br /> | '''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'''<br /> | ||
==Overview== | ==Overview== | ||
To investigate the contribution of the folding cores to the thermodynamic | 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== | ==About this Structure== | ||
1JL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_and_thermus_thermophilus Escherichia coli and thermus thermophilus]. Active as [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] Full crystallographic information is available from [http:// | 1JL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_and_thermus_thermophilus Escherichia coli and thermus thermophilus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berger, J | [[Category: Berger, J M.]] | ||
[[Category: Marqusee, S.]] | [[Category: Marqusee, S.]] | ||
[[Category: Robic, S.]] | [[Category: Robic, S.]] | ||
[[Category: mixed alpha-beta protein]] | [[Category: mixed alpha-beta protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:52 2008'' | ||
Revision as of 14:23, 21 February 2008
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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
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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