Crystallization and preliminary X-ray studies of ferredoxin-NAD(P) + reductase from Chlorobium tepidum

Norifumi Muraki; Daisuke Seo; Tomoo Shiba; Takeshi Sakurai; Genji Kurisu

doi:10.1107/S1744309108003667

Crystallization and preliminary X-ray studies of ferredoxin-NAD(P) ⁺ reductase from Chlorobium tepidum

Norifumi Muraki, Daisuke Seo, Tomoo Shiba, Takeshi Sakurai, Genji Kurisu

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

Ferredoxin-NAD(P)⁺ reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P)⁺ to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C222₁ and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4₁22 or P4₃22. Diffraction data were collected from a form I crystal to 2.4 Å resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.

Original language	English
Pages (from-to)	186-189
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	64
Issue number	3
DOIs	https://doi.org/10.1107/S1744309108003667
Publication status	Published - 2008
Externally published	Yes

Keywords

Ferredoxin-NAD(P) reductase
Photosynthesis

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

Access to Document

10.1107/S1744309108003667

Cite this

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title = "Crystallization and preliminary X-ray studies of ferredoxin-NAD(P) + reductase from Chlorobium tepidum",

abstract = "Ferredoxin-NAD(P)+ reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P)+ to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C2221 and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4122 or P4322. Diffraction data were collected from a form I crystal to 2.4 {\AA} resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.",

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T1 - Crystallization and preliminary X-ray studies of ferredoxin-NAD(P) + reductase from Chlorobium tepidum

AU - Muraki, Norifumi

AU - Seo, Daisuke

AU - Shiba, Tomoo

AU - Sakurai, Takeshi

AU - Kurisu, Genji

PY - 2008

Y1 - 2008

N2 - Ferredoxin-NAD(P)+ reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P)+ to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C2221 and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4122 or P4322. Diffraction data were collected from a form I crystal to 2.4 Å resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.

AB - Ferredoxin-NAD(P)+ reductase (FNR) is a key enzyme that catalyzes the photoreduction of NAD(P)+ to generate NAD(P)H during the final step of the photosynthetic electron-transport chain. FNR from the green sulfur bacterium Chlorobium tepidum is a homodimeric enzyme with a molecular weight of 90 kDa; it shares a high level of amino-acid sequence identity to thioredoxin reductase rather than to conventional plant-type FNRs. In order to understand the structural basis of the ferredoxin-dependency of this unique photosynthetic FNR, C. tepidum FNR has been heterologously expressed, purified and crystallized in two forms. Form I crystals belong to space group C2221 and contain one dimer in the asymmetric unit, while form II crystals belong to space group P4122 or P4322. Diffraction data were collected from a form I crystal to 2.4 Å resolution on the synchrotron-radiation beamline NW12 at the Photon Factory.

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