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2e4p

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{{STRUCTURE_2e4p| PDB=2e4p | SCENE= }}
{{STRUCTURE_2e4p| PDB=2e4p | SCENE= }}
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'''Crystal structure of BphA3 (oxidized form)'''
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===Crystal structure of BphA3 (oxidized form)===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17850818 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17850818}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17850818 17850818]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17850818 17850818]
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Crystallization and preliminary X-ray analysis of the Rieske-type [2Fe-2S] ferredoxin component of biphenyl dioxygenase from Pseudomonas sp. strain KKS102., Senda M, Kimura S, Kishigami S, Senda T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):590-2. Epub 2006 May 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16754990 16754990]
[[Category: Pseudomonas sp.]]
[[Category: Pseudomonas sp.]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Senda, T.]]
[[Category: Senda, T.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:54:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:57:57 2008''

Revision as of 21:58, 27 July 2008

Image:2e4p.png

Template:STRUCTURE 2e4p

Crystal structure of BphA3 (oxidized form)

Template:ABSTRACT PUBMED 17850818

About this Structure

2E4P is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

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

Crystallization and preliminary X-ray analysis of the Rieske-type [2Fe-2S] ferredoxin component of biphenyl dioxygenase from Pseudomonas sp. strain KKS102., Senda M, Kimura S, Kishigami S, Senda T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):590-2. Epub 2006 May 31. PMID:16754990

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