Purification, crystallization and preliminary structural studies of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC), the third enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar typhimurium.

Giraud MF; Whitfield C; Messner PMcMahon SANaismith JHGordon FM

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary structural studies of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC), the third enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar typhimurium.

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Purification, crystallization and preliminary structural studies of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC), the third enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar typhimurium.

机译：净化、结晶和初步的结构的研究5-epimerase dTDP-6-deoxy-D-xylo-4-hexulose 3日(RmlC),第三dTDP-L-rhamnose的酶合成途径,从肠道沙门氏菌血清型沙门氏菌感染。

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L-Rhamnose is an essential component of the cell wall of many pathogenic bacteria. Its precusor, dTDP-L-rhamnose, is synthesized from alpha-D-glucose-1-phosphate and dTTP via a pathway requiring four distinct enzymes: RmlA, RmlB, RmlC and RmlD. RmlC was overexpressed in Escherichia coli. The recombinant protein was purified by a two-step protocol involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated that the recombinant protein is monodisperse. Crystals were obtained using the sitting-drop vapour-diffusion method with ammonium sulfate as precipitant. Diffraction data were collected on a frozen crystal to a resolution of 2.17 A. The crystal belongs to either space group P3121 or P3221, with unit-cell parameters a = b = 71.56, c = 183.53 A and alpha = beta = 90, gamma = 120 degrees.

机译：L-Rhamnose细胞是一个重要的组成部分许多病原菌的墙。dTDP-L-rhamnose,合成alpha-D-glucose-1-phosphate dTTP通过路径需要四个不同的酶:RmlA,RmlB, RmlC RmlD。大肠杆菌。由两步纯化协议涉及阴离子交换和疏水色谱法。动态光散射实验表明重组蛋白是单分散的。使用sitting-drop晶体了vapour-diffusion方法与硫酸铵沉淀剂。冻晶体分辨率为2.17。水晶属于空间群P3121或P3221,晶胞参数a = b = 71.56, cA和α=β= 183.53 = 90,γ= 120度。

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《Acta crystallographica.Section D. Biological crystallography》 |1999年第3期|706-708|共3页
作者
Giraud MF; Whitfield C; Messner PMcMahon SANaismith JHGordon FM;
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Centre for Biomolecular Sciences, Purdie Building, University of St. Andrews, Fife KY16 9ST, Scotland.;

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CHROMATOGRAPHY; Protein Conformation; STRUCTURAL STUDYthymidine diphosphate-L-rhamnoseCell wallCloningthymidine triphosphateFluid pressureSalmonella typhimuriumPathogenic bacteriaCrystallizationRecombinant Proteins;

机译：色谱法;蛋白质构象结构STUDYthymidine diphosphate-L-rhamnoseCellpressureSalmonella typhimuriumPathogenicbacteriaCrystallizationRecombinant蛋白质;

Purification, crystallization and preliminary structural studies of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC), the third enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar typhimurium.

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