dTDP-D-Glucose 4的晶体结构,6-dehydratase (RmlB)鼠伤寒沙门氏菌血清型,第二个dTDP-l-rhamnose通路中的酶。
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阿拉德圣,Giraud MF, Whitfield C, Graninger M, Messner P,奈史密斯JH
dTDP-D-Glucose 4的晶体结构,6-dehydratase (RmlB)鼠伤寒沙门氏菌血清型,第二个dTDP-l-rhamnose通路中的酶。
J杂志。2001年3月16日,307 (1):283 - 95。
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11243820 (在PubMed]
- 文摘
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l-Rhamnose 6-deoxyhexose,发现在各种不同的glycoconjugates病原菌的细胞壁。l-rhamnose的前身是dTDP-l-rhamnose,合成葡萄糖- 1-phosphate和脱氧胸苷三磷酸(dTTP)通过一个通道需要四种酶。明显这个途径不存在在人类和所有四个酶因此代表了潜在的治疗靶点。dTDP-D-glucose 4, 6-dehydratase (RmlB;dTDP-L-rhamnose EC 4.2.1.46)是第二个酶的生物合成途径。鼠伤寒沙门氏菌血清型的结构RmlB 2.47已经决心解决代数余子式NAD(+)绑定。晶体的结构已被提炼r因子20.4%和24.9%的有空值具有良好的立体化学。RmlB为功能单体协会主要是通过四螺旋束通过疏水相互作用发生。每个单体展览一个α/β结构,可分为两个领域。更大的n端结构域结合核苷酸辅因子NAD(+)和由seven-strandedβ褶板阿尔法螺旋包围。 The smaller C-terminal domain is responsible for binding the sugar substrate dTDP-d-glucose and contains four beta-strands and six alpha-helices. The two domains meet to form a cavity in the enzyme. The highly conserved active site Tyr(167)XXXLys(171) catalytic couple and the GlyXGlyXXGly motif at the N terminus characterise RmlB as a member of the short-chain dehydrogenase/reductase extended family. The quaternary structure of RmlB and its similarity to a number of other closely related short-chain dehydrogenase/reductase enzymes have enabled us to propose a mechanism of catalysis for this important enzyme.