Beckham Katherine S H, Byron Olwyn, Roe Andrew J, Gabrielsen Mads
Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Sir Graeme Davies Building, Glasgow G12 8QQ, Scotland.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. doi: 10.1107/S1744309112011487. Epub 2012 Apr 20.
Thiol peroxidase (Tpx) is an atypical 2-Cys peroxiredoxin, which has been suggested to be important for cell survival and virulence in Gram-negative pathogens. The structure of a catalytically inactive version of this protein in an orthorhombic crystal form has been determined by molecular replacement. Structural alignments revealed that Tpx is conserved. Analysis of the crystal packing shows that the linker region of the affinity tag is important for formation of the crystal lattice.
硫醇过氧化物酶（Tpx）是一种非典型的2-半胱氨酸过氧化物酶，有人认为它对革兰氏阴性病原体的细胞存活和毒力很重要。已通过分子置换确定了这种蛋白质的催化无活性形式在正交晶系晶体形式中的结构。结构比对显示Tpx是保守的。晶体堆积分析表明，亲和标签的连接区对晶格的形成很重要。
