普通脱硫弧菌希登伯勒氏亚种膜结合复合物细胞色素c亚硝酸还原酶的结晶及初步结构测定
Crystallization and preliminary structure determination of the membrane-bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris Hildenborough.
作者信息
Rodrigues M L, Oliveira T, Matias P M, Martins I C, Valente F M A, Pereira I A C, Archer M
机构信息
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, ITQB-UNL, Av. República, Apt. 127, 2781-901 Oeiras, Portugal.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):565-8. doi: 10.1107/S1744309106016629. Epub 2006 May 31.
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 A resolution. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 79.5, b = 256.7, c = 578.2 A. 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.
摘要
从希登伯勒脱硫弧菌中分离出的细胞色素c亚硝酸盐还原酶（cNiR）是一种由NrfA和NrfH亚基组成的膜结合复合物。催化亚基NrfA是一种可溶性的五血红素细胞色素c，形成一个约120 kDa的生理性二聚体。电子供体亚基NrfH是一种分子量约为18 kDa的膜锚定四血红素细胞色素c，属于喹啉脱氢酶的NapC/NirT家族，目前尚无其结构信息。使用聚乙二醇4000（PEG 4K）作为沉淀剂，获得了用十二烷基麦芽糖苷洗涤剂（DDM）溶解的天然cNiR膜复合物晶体。在瑞士光源处测量了反常衍射数据，分辨率达到2.3 Å。晶体属于正交空间群P2(1)2(1)2(1)，晶胞参数a = 79.5，b = 256.7，c = 578.2 Å。结合分子置换法和多波长反常散射（MAD）法解析了其结构。所呈现的数据表明，希登伯勒脱硫弧菌cNiR每个NrfA二聚体含有一个NrfH亚基。
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