Omi Rie, Goto Masaru, Nakagawa Noriko, Miyahara Ikuko, Hirotsu Ken
Department of Chemistry, Graduate School of Science, Osaka City University, Japan.
Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):574-6. doi: 10.1107/S0907444904000277. Epub 2004 Feb 25.
Histidinol phosphate phosphatase (HisPPase) catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. A recombinant form of the histidinol phosphate phosphatase from Thermus thermophilus HB8 has been expressed in Escherichia coli, purified and crystallized in two crystal forms by the hanging-drop vapour-diffusion technique. Crystal form I belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 84.8, b = 97.2, c = 74.9 A, and crystal form II belongs to the orthorhombic space group C222(1), with unit-cell parameters a = 76.9, b = 157.6, c = 116.7 A. The crystals probably contain two monomers in the asymmetric unit, with V(M) values of 2.57 A(3) Da(-1) for form I and 2.96 A(3) Da(-1) for form II. X-ray data have been collected to 1.70 and 1.75 A resolution for crystal forms I and II, respectively.
磷酸组氨醇磷酸酶（HisPPase）催化组氨酸生物合成的第八步反应，即磷酸-L-组氨醇发生去磷酸化反应生成组氨醇。嗜热栖热菌HB8来源的磷酸组氨醇磷酸酶的重组形式已在大肠杆菌中表达，并通过悬滴气相扩散技术纯化并结晶为两种晶体形式。晶型I属于正交晶系空间群P2(1)2(1)2，晶胞参数a = 84.8，b = 97.2，c = 74.9 Å；晶型II属于正交晶系空间群C222(1)，晶胞参数a = 76.9，b = 157.6，c = 116.7 Å。不对称单元中每个晶体可能含有两个单体，晶型I的V(M)值为2.57 Å(3) Da(-1)，晶型II的V(M)值为2.96 Å(3) Da(-1)。晶型I和晶型II的X射线数据分别已收集至1.70 Å和1.75 Å分辨率。
