嗜热栖热菌OT3中一种假定的UDP-N-乙酰-D-甘露糖胺脱氢酶的纯化、结晶及初步X射线衍射研究
Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3.
作者信息
Lokanath Neratur K, Pampa Kudigana J, Kamiya Toshimi, Kunishima Naoki
机构信息
Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):412-4. doi: 10.1107/S1744309107016685. Epub 2007 Apr 14.
Abstract
A putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3, an essential enzyme for polysaccharide biosynthesis, has been overexpressed in Escherichia coli and purified. Crystals were obtained using the oil-microbatch method at 291 K. A native data set extending to 1.8 A resolution has been collected and processed in space group P2(1). Assuming the presence of a dimer in the asymmetric unit, the V(M) value is calculated to be 2.3 A3 Da(-1), which is consistent with the result of a dynamic light-scattering experiment that shows a dimeric state of the protein in solution.
摘要
来自嗜热栖热菌OT3的一种假定的UDP-N-乙酰-D-甘露糖胺脱氢酶，它是多糖生物合成中的一种必需酶，已在大肠杆菌中过表达并纯化。采用油微批量法在291 K下获得了晶体。在空间群P2(1)中收集并处理了分辨率达到1.8 Å的天然数据集。假设不对称单元中存在二聚体，计算出的V(M)值为2.3 Å3 Da(-1)，这与动态光散射实验结果一致，该实验表明该蛋白质在溶液中呈二聚体状态。
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