Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium.
Primary structure and crystallization of orotate phosphoribosyltransferase from Salmonella typhimurium.
复制标题
鼠伤寒沙门氏菌乳清酸磷酸核糖基转移酶的一级结构和结晶。
DOI：
10.1006/jmbi.1993.1244
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发表时间：
1993
影响因子：
5.6
通讯作者：
Grubmeyer,C
中科院分区：
文献类型：
--
作者：
Scapin,G;Sacchettini,JC;Dessen,A;Bhatia,M;Grubmeyer,C
Orotate phosphoribosyltransferase (OPRTase; EC 2.4.2.10) catalyzes phosphoribosyl group transfer between alpha-d-5-phosphoribosyl-1-pyrophosphate and orotate to form orotidine-5′-monophosphate and pyrophosphate, the nucleotide-forming step in pyrimidine biosynthesis. It is one of ten PRTases that perform viral roles inde novoand salvage pathways for purine, pyrimidine and pyridine nucleotides. Although the PRTases are important drug targets, they are poorly understood mechanistically, and no three-dimensional structures exist. Here, we report the complete sequence of theSalmonella typhimurium pyrEgene and the deduced sequence of the OPRTase gene product. OPRTase forms tetragonal crystals from polyethylene glycol solutions; these crystals diffract to better than 2 Å resolution, and are stable to radiation damage. The space group isP41212 (orP43212) with unit cell dimensions ofa=b= 48·5 Å,c= 210·5 Å, and α = β = γ = 90°. A crystalline form of the selenomethionine derivative of the protein is also reported.
