1dvv
From Proteopedia
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|PDB= 1dvv |SIZE=350|CAPTION= <scene name='initialview01'>1dvv</scene> | |PDB= 1dvv |SIZE=350|CAPTION= <scene name='initialview01'>1dvv</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Tanimoto, Y.]] | [[Category: Tanimoto, Y.]] | ||
[[Category: Uchiyama, S.]] | [[Category: Uchiyama, S.]] | ||
| - | [[Category: HEM]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: stability]] | [[Category: stability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:49 2008'' |
Revision as of 16:49, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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