2gr0: Difference between revisions

Revision as of 06:02, 29 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:2gr0.png

Template:STRUCTURE 2gr0

Crystal structure of Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex)Crystal structure of Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex)

Template:ABSTRACT PUBMED 17850818

About this StructureAbout this Structure

2GR0 is a Single protein structure of sequence from Pseudomonas sp. kks102. Full crystallographic information is available from OCA.

ReferenceReference

Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin., Senda M, Kishigami S, Kimura S, Fukuda M, Ishida T, Senda T, J Mol Biol. 2007 Oct 19;373(2):382-400. Epub 2007 Aug 19. PMID:17850818

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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 Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex)'''
+===Crystal structure of Ferredoxin reductase, BphA4 (oxidized form, NAD+ complex)===
-==Overview==
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-The electron transfer system of the biphenyl dioxygenase BphA, which is derived from Acidovorax sp. (formally Pseudomonas sp.) strain KKS102, is composed of an FAD-containing NADH-ferredoxin reductase (BphA4) and a Rieske-type [2Fe-2S] ferredoxin (BphA3). Biochemical studies have suggested that the whole electron transfer process from NADH to BphA3 comprises three consecutive elementary electron-transfer reactions, in which BphA3 and BphA4 interact transiently in a redox-dependent manner. Initially, BphA4 receives two electrons from NADH. The reduced BphA4 then delivers one electron each to the [2Fe-2S] cluster of the two BphA3 molecules through redox-dependent transient interactions. The reduced BphA3 transports the electron to BphA1A2, a terminal oxygenase, to support the activation of dioxygen for biphenyl dihydroxylation. In order to elucidate the molecular mechanisms of the sequential reaction and the redox-dependent interaction between BphA3 and BphA4, we determined the crystal structures of the productive BphA3-BphA4 complex, and of free BphA3 and BphA4 in all the redox states occurring in the catalytic cycle. The crystal structures of these reaction intermediates demonstrated that each elementary electron transfer induces a series of redox-dependent conformational changes in BphA3 and BphA4, which regulate the interaction between them. In addition, the conformational changes induced by the preceding electron transfer seem to induce the next electron transfer. The interplay of electron transfer and induced conformational changes seems to be critical to the sequential electron-transfer reaction from NADH to BphA3.
+The line below this paragraph, {{ABSTRACT_PUBMED_17850818}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17850818}}
 ==About this Structure==
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 [[Category: Flavoprotein]]
 [[Category: Oxidoreductase]]
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