Kukimoto-Niino Mutsuko, Shibata Rie, Murayama Kazutaka, Hamana Hiroaki, Nishimoto Madoka, Bessho Yoshitaka, Terada Takaho, Shirouzu Mikako, Kuramitsu Seiki, Yokoyama Shigeyuki
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Protein Sci. 2005 Mar;14(3):823-7. doi: 10.1110/ps.041229405. Epub 2005 Feb 2.
TT1426, from Thermus thermophilus HB8, is a conserved hypothetical protein with a predicted phosphoribosyltransferase (PRTase) domain, as revealed by a Pfam database search. The 2.01 A crystal structure of TT1426 has been determined by the multiwavelength anomalous dispersion (MAD) method. TT1426 comprises a core domain consisting of a central five-stranded beta sheet surrounded by four alpha-helices, and a subdomain in the C terminus. The core domain structure resembles those of the type I PRTase family proteins, although a significant structural difference exists in an inserted 43-residue region. The C-terminal subdomain corresponds to the "hood," which contains a substrate-binding site in the type I PRTases. The hood structure of TT1426 differs from those of the other type I PRTases, suggesting the possibility that TT1426 binds an unknown substrate. The structure-based sequence alignment provides clues about the amino acid residues involved in catalysis and substrate binding.
TT1426来自嗜热栖热菌HB8,是一种保守的假定蛋白,通过Pfam数据库搜索发现它具有一个预测的磷酸核糖基转移酶(PRTase)结构域。TT1426的晶体结构为2.01埃,已通过多波长反常色散(MAD)方法确定。TT1426包含一个核心结构域,该结构域由一个中央的五链β折叠片层和周围的四个α螺旋组成,以及一个位于C末端的亚结构域。核心结构域的结构类似于I型PRTase家族蛋白的结构,尽管在一个插入的43个残基区域存在显著的结构差异。C末端亚结构域对应于“I型PRTases”中的“帽”,其中包含一个底物结合位点。TT1426的帽结构与其他I型PRTases的帽结构不同,这表明TT1426可能结合一种未知底物。基于结构的序列比对为参与催化和底物结合的氨基酸残基提供了线索。