1smm: Difference between revisions

Revision as of 12:46, 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:1smm.png

Template:STRUCTURE 1smm

Crystal Structure of Cp Rd L41A mutant in oxidized stateCrystal Structure of Cp Rd L41A mutant in oxidized state

Template:ABSTRACT PUBMED 15067525

About this StructureAbout this Structure

1SMM is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.

ReferenceReference

The unique hydrogen bonded water in the reduced form of Clostridium pasteurianum rubredoxin and its possible role in electron transfer., Park IY, Youn B, Harley JL, Eidsness MK, Smith E, Ichiye T, Kang C, J Biol Inorg Chem. 2004 Jun;9(4):423-8. Epub 2004 Apr 6. PMID:15067525

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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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-'''Crystal Structure of Cp Rd L41A mutant in oxidized state'''
+===Crystal Structure of Cp Rd L41A mutant in oxidized state===
-==Overview==
+<!--
-Rubredoxin is a small iron-sulfur (FeS4) protein involved in oxidation-reduction reactions. The side chain of Leu41 near the iron-sulfur center has two conformations, which we suggested previously serve as a gate for a water molecule during the electron transfer process. To establish the role of residue 41 in electron transfer, an [L41A] mutant of Clostridium pasteurianum rubredoxin was constructed and crystallized in both oxidation states. Despite the lack of the gating side chain in this protein, the structure of the reduced [L41A] rubredoxin reveals a specific water molecule in the same position as observed in the reduced wild-type rubredoxin. In contrast, both the wild-type and [L41A] rubredoxins in the oxidized state do not have water molecules in this location. The reduction potential of the [L41A] variant was approximately 50 mV more positive than wild-type. Based on these observations, it is proposed that the site around the Sgamma of Cys9 serves as a port for an electron acceptor. Lastly, the Fe-S distances of the reduced rubredoxin are expanded, while the hydrogen bonds between Sgamma of the cysteines and the backbone amide nitrogens are shortened compared to its oxidized counterpart. This small structural perturbation in the Fe(II)/Fe(III) transition is closely related to the small energy difference which is important in an effective electron transfer agent.
+The line below this paragraph, {{ABSTRACT_PUBMED_15067525}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15067525}}
 ==About this Structure==
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 [[Category: Youn, B.]]
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