Karplus P Andrew, Hall Andrea
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.
Subcell Biochem. 2007;44:41-60. doi: 10.1007/978-1-4020-6051-9_3.
Peroxiredoxins (Prxs) are ubiquitous proteins that use an active site Cys residue to reduce hydroperoxides. Structural studies since the first Prx structure was determined in 1998 have produced 35 crystal structures of wild type and mutant Prxs with at least one representative structure from each of the five major evolutionary subfamilies of Prxs. These structures have yielded a great deal of knowledge about Prx structure and structure-function relations, revealing fascinating variations in quaternary structure and details of the fully-folded and locally-unfolded conformations that are involved in the catalytic cycle of all Prxs.
过氧化物酶（Prxs）是普遍存在的蛋白质，它们利用活性位点的半胱氨酸残基来还原氢过氧化物。自1998年确定首个Prx结构以来的结构研究，已产生了35个野生型和突变型Prxs的晶体结构，其中五个主要进化亚家族的Prxs各至少有一个代表性结构。这些结构产生了大量关于Prx结构及其结构-功能关系的知识，揭示了四级结构中迷人的变化以及所有Prxs催化循环中涉及的完全折叠和局部未折叠构象的细节。
