2i8f: Difference between revisions
New page: left|200px<br /><applet load="2i8f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i8f" /> '''Solution Conformation of the H47A Mutant of ... |
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'''Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551'''<br /> | '''Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2I8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2I8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I8F OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:42:29 2008'' | ||
Revision as of 14:42, 23 January 2008
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Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551
OverviewOverview
In the cytochrome c-551 family, the heme 17-propionate caboxylate group is, always hydrogen bonded to an invariant Trp56 and conserved residues (His, and Arg mainly, Lys occasionally) at position 47. The mutation of His47 to, Ala47 for Pseudomas stutzeri ZoBell cytochrome c-551 removes this, otherwise invariant hydrogen bond. The solution structure of ferrous H47A, has been solved based upon NMR-derived constraints. Results indicate the, mutant has very similar main chain folding compared to wild-type. However, less efficient packing of residues in the mutant surrounding the heme, propionates leads to more solvent exposure for both propionate groups, which may account for decreased stability of the mutant. The mutant has a, reduction potential different from wild type and furthermore, the pH, dependence of this potential is not the same as for wild type. The, structure of the mutant suggests that these changes are related to the, loss of the residue 47-propionate hydrogen bond and the loss of charge on, the side chain of residue 47.
About this StructureAbout this Structure
2I8F is a Single protein structure of sequence from Pseudomonas stutzeri with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution Conformation of the His 47 to Ala 47 Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551., Liang Q, Miller GT, Beeghley CA, Graf CB, Timkovich R, Biophys J. 2007 May 11;. PMID:17496029
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