1w40
From Proteopedia
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| - | [[Image:1w40.gif|left|200px]] | + | [[Image:1w40.gif|left|200px]] |
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| - | '''T. CELER L30E K9A VARIANT''' | + | {{Structure |
| + | |PDB= 1w40 |SIZE=350|CAPTION= <scene name='initialview01'>1w40</scene>, resolution 2.03Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''T. CELER L30E K9A VARIANT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W40 is a [ | + | 1W40 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W40 OCA]. |
==Reference== | ==Reference== | ||
| - | Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e., Lee CF, Allen MD, Bycroft M, Wong KB, J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:[http:// | + | Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e., Lee CF, Allen MD, Bycroft M, Wong KB, J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15811378 15811378] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermococcus celer]] | [[Category: Thermococcus celer]] | ||
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[[Category: Lee, K M.]] | [[Category: Lee, K M.]] | ||
[[Category: Wong, K B.]] | [[Category: Wong, K B.]] | ||
| - | [[Category: electrostatic | + | [[Category: electrostatic interaction]] |
[[Category: protein engineering]] | [[Category: protein engineering]] | ||
[[Category: ribosomal protein]] | [[Category: ribosomal protein]] | ||
[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:51:49 2008'' |
Revision as of 12:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
T. CELER L30E K9A VARIANT
Overview
The origin of reduced heat capacity change of unfolding (DeltaC(p)) commonly observed in thermophilic proteins is controversial. The established theory that DeltaC(p) is correlated with change of solvent-accessible surface area cannot account for the large differences in DeltaC(p) observed for thermophilic and mesophilic homologous proteins, which are very similar in structures. We have determined the protein stability curves, which describe the temperature dependency of the free energy change of unfolding, for a thermophilic ribosomal protein L30e from Thermococcus celer, and its mesophilic homologue from yeast. Values of DeltaC(p), obtained by fitting the free energy change of unfolding to the Gibbs-Helmholtz equation, were 5.3 kJ mol(-1) K(-1) and 10.5 kJ mol(-1) K(-1) for T.celer and yeast L30e, respectively. We have created six charge-to-neutral mutants of T.celer L30e. Removal of charges at Glu6, Lys9, and Arg92 decreased the melting temperatures of T.celer L30e by approximately 3-9 degrees C, and the differences in melting temperatures were smaller with increasing concentration of salt. These results suggest that these mutations destabilize T.celer L30e by disrupting favorable electrostatic interactions. To determine whether electrostatic interactions contribute to the reduced DeltaC(p) of the thermophilic protein, we have determined DeltaC(p) for wild-type and mutant T.celer L30e by Gibbs-Helmholtz and by van't Hoff analyses. A concomitant increase in DeltaC(p) was observed for those charge-to-neutral mutants that destabilize T.celer L30e by removing favorable electrostatic interactions. The crystal structures of K9A, E90A, and R92A, were determined, and no structural change was observed. Taken together, our results support the conclusion that electrostatic interactions contribute to the reduced DeltaC(p) of T.celer L30e.
About this Structure
1W40 is a Single protein structure of sequence from Thermococcus celer. Full crystallographic information is available from OCA.
Reference
Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e., Lee CF, Allen MD, Bycroft M, Wong KB, J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:15811378
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