Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea
Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea
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DOI：
10.1107/s1744309109046119
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发表时间：
2009-12-01
影响因子：
0.9
通讯作者：
Wilmot, Carrie M.
中科院分区：
文献类型：
--
作者：
Cedervall, Peder E.;Hooper, Alan B.;Wilmot, Carrie M.
羟胺氧化还原酶（HAO）是一种来自欧洲亚硝化单胞菌（Nitrosomonaseuropaea）的同源三聚体蛋白，催化羟胺氧化为亚硝酸盐。每个单体的分子量为67.1 kDa，含有7个C型血红素和1个血红素P460，其卟啉环与相邻亚基的酪氨酸残基共价连接。1997年，HAO首次结晶并以2.8埃的分辨率进行结构表征。其结构属于P6（3）空间群，存在半面体孪晶。在这里，提出了一种结晶过程，产生属于空间群P2（1）2（1）2，衍射到2.25埃的分辨率和包含一个三聚体的不对称单元的非孪晶晶体。晶胞参数为a = 140.7，B = 142.6，c = 107.4埃。
Hydroxylamine oxidoreductase (HAO) from Nitrosomonas europaea is a homotrimeric protein that catalyzes the oxidation of hydroxylamine to nitrite. Each monomer, with a molecular weight of 67.1 kDa, contains seven c-type hemes and one heme P460, the porphyrin ring of which is covalently linked to a tyrosine residue from an adjacent subunit. HAO was first crystallized and structurally characterized at a resolution of 2.8 angstrom in 1997. The structure was solved in space group P6(3) and suffered from merohedral twinning. Here, a crystallization procedure is presented that yielded untwinned crystals belonging to space group P2(1)2(1)2, which diffracted to 2.25 angstrom resolution and contained one trimer in the asymmetric unit. The unit-cell parameters were a = 140.7, b = 142.6, c = 107.4 angstrom.