2i8f: Difference between revisions

Revision as of 17:16, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2i8f.png

Template:STRUCTURE 2i8f

Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551

Template:ABSTRACT PUBMED 17496029

About this StructureAbout this Structure

2I8F is a Single protein structure of sequence from Pseudomonas stutzeri. Full experimental 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 Sep 1;93(5):1700-6. Epub 2007 May 11. PMID:17496029

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551'''
+===Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551===
-==Overview==
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-In the cytochrome c-551 family, the heme 17-propionate caboxylate group is always hydrogen bonded to an invariant Trp-56 and conserved residues (His and Arg mainly, Lys occasionally) at position 47. The mutation of His-47 to Ala-47 for Pseudomas stutzeri ZoBell cytochrome c-551 removes this otherwise invariant hydrogen bond. The solution structure of ferrous H47A has been solved based on NMR-derived constraints. Results indicate that 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17496029}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17496029 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17496029}}
 ==About this Structure==
-I8F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I8F OCA].
+I8F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I8F OCA].
 ==Reference==
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 [[Category: Cytochrome]]
 [[Category: Helix-turn-helix]]
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