Jin Tengchuan, Guo Feng, Wang Yang, Zhang Yuzhu
Department of Biological and Chemical Sciences, Illinois Institute of Technology, 3101 South Dearborn Street, Chicago, IL 60616, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):223-7. doi: 10.1107/S1744309113000973. Epub 2013 Feb 22.
TXNL4A (thioredoxin-like 4A) is an essential protein conserved from yeast to humans and is a component of the pre-mRNA splicing machinery. TXNL4B was identified as a TXNL4-family protein that also interacts with Prp6, an integral component of the U4/U6·U5 tri-snRNP complex, and has been shown to function in pre-mRNA splicing. A crystal structure of TXNL4B was determined at 1.33 Å resolution and refined to an Rwork of 0.13 and an Rfree of 0.18 with one native dimer in the asymmetric unit. Residues 1-33 of TXNL4B have previously been reported to be responsible for its interaction with Prp6. However, this region extends to the β-sheet core of the thioredoxin-fold structure of TXNL4B. This suggests that the interpretation of the previously reported GST pull-down results without considering the structure and stability of TXNL4B is debatable.
TXNL4A（硫氧还蛋白样4A）是一种从酵母到人类都保守的必需蛋白，是前体mRNA剪接机制的一个组成部分。TXNL4B被鉴定为一种TXNL4家族蛋白，它也与U4/U6·U5三小核核糖核蛋白复合体的一个组成部分Prp6相互作用，并且已被证明在前体mRNA剪接中发挥作用。TXNL4B的晶体结构在1.33 Å分辨率下测定，并精修至工作R因子为0.13，自由R因子为0.18，不对称单元中有一个天然二聚体。TXNL4B的1至33位残基先前已被报道负责其与Prp6的相互作用。然而，该区域延伸至TXNL4B硫氧还蛋白折叠结构的β-折叠核心。这表明在不考虑TXNL4B的结构和稳定性的情况下对先前报道的谷胱甘肽S-转移酶下拉结果的解释是有争议的。
