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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The purification, crystallization and structural elucidation of dTDP-D-glucose 4,6-dehydratase (RmlB), the second enzyme of the dTDP-L-rhamnose synthesis pathway from Salmonella enterica serovar Typhimurium
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The purification, crystallization and structural elucidation of dTDP-D-glucose 4,6-dehydratase (RmlB), the second enzyme of the dTDP-L-rhamnose synthesis pathway from Salmonella enterica serovar Typhimurium

机译：净化,结晶和结构说明dTDP-D-glucose 4, 6-dehydratase(RmlB),第二个dTDP-L-rhamnose的酶从肠道沙门氏菌血清合成途径型沙门氏菌感染

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摘要

dTDP-D-glucose 4-6-dehydratase (RmlB) is the second of four enzymes involved in the dTDP-L-rhamnose pathway and catalyzes the dehydration of dTDP-D-glucose to dTDP-4-keto-6-deoxy-D-glucose. The ultimate product of the pathway, dTDP-L-rhamnose, is the precursor of L-rhamnose, which is a key component of the cell wall of many pathogenic bacteria. RmlB from Salmonella enterica serovar Typhimurium has been overexpressed and purified, and crystals of the enzyme have been grown using the sitting-drop vapour-diffusion technique with lithium sulfate as precipitant. Diffraction data have been obtained to a resolution of 2.8 A on a single frozen RmlB crystal which belongs to space group P2_1, with unit-cell parameters a = 111.85, b = 87.77, c = 145.66 A, β = 131.53°. The asymmetric unit contains four monomers in the form of two RmlB dimers with a solvent content of 62%. A molecular-replacement solution has been obtained and the model is currently being refined.
机译：dTDP-D-glucose 4-6-dehydratase (RmlB)第二次四种酶的参与dTDP-L-rhamnose通路和催化脱水的dTDP-D-glucosedTDP-4-keto-6-deoxy-D-glucose。产品的途径,dTDP-L-rhamnose,L-rhamnose的前兆,这是一个关键组成部分许多病原菌的细胞壁。RmlB鼠伤寒沙门氏菌血清型过表达和纯化,水晶吗酶的使用sitting-drop vapour-diffusion技术与硫酸锂作为沉淀剂。取得了2.8的决议吗单冻RmlB晶体属于空间集团P2_1,晶胞参数= 111.85,b = 87.77, c = 145.66,β= 131.53°。不对称单元中包含四个单体形式的两个RmlB溶剂含量的二聚体62%。模型是目前获得的雅致。

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