Zhao Rui, Shen Jingping, Green Michael R, MacMorris Margaret, Blumenthal Thomas
Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Aurora, Colorado 80045, USA.
Structure. 2004 Aug;12(8):1373-81. doi: 10.1016/j.str.2004.06.006.
UAP56 is an essential eukaryotic pre-mRNA splicing factor and mRNA export factor. The mechanisms of its functions are not well understood. We determined the crystal structures of the N- and C-terminal domains of human UAP56 (comprising 90% of the full-length UAP56) at 1.9 A resolution. The two domains each have a RecA-like fold and are connected by a flexible linker. The overall fold of each domain is highly similar to the corresponding domains of eIF4A (a prototypic DExD/H-box protein), with differences at the loops and termini. This structural similarity suggests that UAP56 is likely to possess ATPase and helicase activity similar to eIF4A. The NTP binding pocket of UAP56 is occupied by a citrate ion, mimicking the phosphates of NTP and retaining the P loop in an open conformation. The crystal structure of the N-terminal domain of UAP56 also reveals a dimer interface that is potentially important for UAP56's function.
UAP56是一种重要的真核生物前体mRNA剪接因子和mRNA输出因子。其功能机制尚未完全了解。我们以1.9埃的分辨率确定了人UAP56的N端和C端结构域（占全长UAP56的90%）的晶体结构。这两个结构域各自具有类似RecA的折叠结构，并通过一个柔性连接子相连。每个结构域的整体折叠与eIF4A（一种典型的DExD/H盒蛋白）的相应结构域高度相似，只是在环和末端存在差异。这种结构相似性表明UAP56可能具有与eIF4A类似的ATPase和螺旋酶活性。UAP56的NTP结合口袋被一个柠檬酸离子占据，模拟了NTP的磷酸基团，并使P环保持开放构象。UAP56 N端结构域的晶体结构还揭示了一个二聚体界面，这可能对UAP56的功能很重要。
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