View source for 1jl2

[[Image:1jl2.gif|left|200px]]

 {{Structure
|PDB= 1jl2 |SIZE=350|CAPTION= <scene name='initialview01'>1jl2</scene>, resolution 1.76&Aring;
|SITE= 
|LIGAND= 
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= RNase H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Escherichia coli and Thermus thermophilus])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jl2 OCA], [http://www.ebi.ac.uk/pdbsum/1jl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jl2 RCSB]</span>
}}

'''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 [http://en.wikipedia.org/wiki/Escherichia_coli_and_thermus_thermophilus Escherichia coli and thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL2 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:[http://www.ncbi.nlm.nih.gov/pubmed/11790848 11790848]
[[Category: Escherichia coli and thermus thermophilus]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Berger, J M.]]
[[Category: Marqusee, S.]]
[[Category: Robic, S.]]
[[Category: mixed alpha-beta protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:15 2008''