1jl2

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[[Image:1jl2.gif|left|200px]]
[[Image:1jl2.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jl2 |SIZE=350|CAPTION= <scene name='initialview01'>1jl2</scene>, resolution 1.76&Aring;
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The line below this paragraph, containing "STRUCTURE_1jl2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= RNase H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Escherichia coli and Thermus thermophilus])
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|DOMAIN=
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{{STRUCTURE_1jl2| PDB=1jl2 | SCENE= }}
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|RELATEDENTRY=
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|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>
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}}
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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'''
'''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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[[Category: Marqusee, S.]]
[[Category: Marqusee, S.]]
[[Category: Robic, S.]]
[[Category: Robic, S.]]
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[[Category: mixed alpha-beta protein]]
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[[Category: Mixed alpha-beta protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:21:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:15 2008''
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Revision as of 18:21, 2 May 2008

Template:STRUCTURE 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


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

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