1dvv
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1dvv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvv" /> '''SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT O...)
Next diff →
Revision as of 11:30, 20 November 2007
|
SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM PSEUDOMONAS AERUGINOSA
Overview
Mesophilic cytochrome c(551) of Pseudomonas aeruginosa (PA c(551)) became, as stable as its thermophilic counterpart, Hydrogenobacter thermophilus, cytochrome c(552) (HT c(552)), through only five amino acid substitutions., The five residues, distributed in three spatially separated regions, were, selected and mutated with reference to the corresponding residues in HT, c(552) through careful structure comparison. Thermodynamic analysis, indicated that the stability of the quintuple mutant of PA c(551) could be, partly attained through an enthalpic factor. The solution structure of the, mutant showed that, as in HT c(552), there were tighter side chain, packings in the mutated regions. Furthermore, the mutant had an increased, total accessible surface area, resulting in great negative hydration free, energy. Our results provide a novel example of protein stabilization in, that limited amino acid substitutions can confer the overall stability of, a natural highly thermophilic protein upon a mesophilic molecule.
About this Structure
1DVV is a Single protein structure of sequence from Pseudomonas aeruginosa with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart., Hasegawa J, Uchiyama S, Tanimoto Y, Mizutani M, Kobayashi Y, Sambongi Y, Igarashi Y, J Biol Chem. 2000 Dec 1;275(48):37824-8. PMID:10918067
Page seeded by OCA on Tue Nov 20 13:37:46 2007
