Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough

M. L. Rodrigues; T. Oliveira; P. M. Matias; I. C. Martins; Filipa Valente; I. A.C. Pereira; M. Archer

doi:10.1107/S1744309106016629

Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough

M. L. Rodrigues, T. Oliveira, P. M. Matias, I. C. Martins, Filipa Valente, I. A.C. Pereira, M. Archer

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

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Abstract

The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.

Original language	English
Pages (from-to)	565-568
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	6
DOIs	https://doi.org/10.1107/S1744309106016629
Publication status	Published - 1 Jun 2006

Keywords

nitrate reductase (cytochrome)
protein subunit
cytochrome a1
cytochrome c1
membrane protein
nitrate reductase

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Rodrigues, M. L., Oliveira, T., Matias, P. M., Martins, I. C., Valente, F., Pereira, I. A. C., & Archer, M. (2006). Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(6), 565-568. https://doi.org/10.1107/S1744309106016629

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title = "Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough",

abstract = "The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 {\AA} resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 {\AA}. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.",

keywords = "nitrate reductase (cytochrome), protein subunit, cytochrome a1, cytochrome c1, membrane protein, nitrate reductase",

author = "Rodrigues, {M. L.} and T. Oliveira and Matias, {P. M.} and Martins, {I. C.} and Filipa Valente and Pereira, {I. A.C.} and M. Archer",

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Rodrigues, ML, Oliveira, T , Matias, PM, Martins, IC, Valente, F, Pereira, IAC & Archer, M 2006, 'Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 6, pp. 565-568. https://doi.org/10.1107/S1744309106016629

Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough. / Rodrigues, M. L.; Oliveira, T.; Matias, P. M. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 6, 01.06.2006, p. 565-568.

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

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N2 - The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.

AB - The cytochrome c nitrite reductase (cNiR) isolated from Desulfovibrio vulgaris Hildenborough is a membrane-bound complex formed of NrfA and NrfH subunits. The catalytic subunit NrfA is a soluble pentahaem cytochrome c that forms a physiological dimer of about 120 kDa. The electron-donor subunit NrfH is a membrane-anchored tetrahaem cytochrome c of about 18 kDa molecular weight and belongs to the NapC/NirT family of quinol dehydrogenases, for which no structures are known. Crystals of the native cNiR membrane complex, solubilized with dodecylmaltoside detergent (DDM), were obtained using PEG 4K as precipitant. Anomalous diffraction data were measured at the Swiss Light Source to 2.3 Å resolution. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 Å. Molecular-replacement and MAD methods were combined to solve the structure. The data presented reveal that D. vulgaris cNiR contains one NrfH subunit per NrfA dimer.

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SN - 1744-3091

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EP - 568

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 6

ER -

Rodrigues ML, Oliveira T , Matias PM, Martins IC, Valente F, Pereira IAC et al. Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 Jun 1;62(6):565-568. doi: 10.1107/S1744309106016629

Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough

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