1dvv

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvv OCA], [http://www.ebi.ac.uk/pdbsum/1dvv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dvv RCSB]</span>
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'''SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM PSEUDOMONAS AERUGINOSA'''
'''SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM PSEUDOMONAS AERUGINOSA'''
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[[Category: Tanimoto, Y.]]
[[Category: Tanimoto, Y.]]
[[Category: Uchiyama, S.]]
[[Category: Uchiyama, S.]]
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[[Category: cytochrome c]]
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[[Category: Cytochrome c]]
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[[Category: stability]]
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[[Category: Stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:20:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:49 2008''
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Revision as of 11:20, 2 May 2008

Image:1dvv.jpg

Template:STRUCTURE 1dvv

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. 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 Fri May 2 14:20:42 2008

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