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首页> 外文期刊>Acta crystallographica.Section D Biological crystallography. >Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway
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Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway

机译：幽门螺杆菌的结构性酶学methylthioadenosine核苷酶的futalosine通路

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摘要

The recently discovered futalosine pathway is a promising target for the development of new antibiotics. The enzymes involved in this pathway are crucial for the biosynthesis of the essential prokaryotic respiratory compound menaquinone, and as the pathway is limited to few bacterial species such as the gastric pathogen Helicobacter pylori it is a potential target for specific antibiotics. In this report, the crystal structure of an H. pylori methylthioadenosine nucleosidase (MTAN; an enzyme with broad specificity and activity towards 6-amino-6-deoxyfutalosine), which is involved in the second step of menaquinone biosynthesis, has been elucidated at a resolution of 1.76 ? and refined with R factors of R work = 17% and R free = 21%. Activity studies on the wild type and active-site mutants show that the hydrolysis of 6-amino-6-deoxyfutalosine follows a mechanism similar to that of Escherichia coli MTAN. Further evidence for this mode of action is supplied by the crystal structures of active-site mutants. Through the use of reaction intermediates, the structures give additional evidence for the previously proposed nucleosidase mechanism. These structures and the confirmed reaction mechanism will provide a structural basis for the design of new inhibitors targeting the futalosine pathway.
机译：最近发现futalosine通路是a有前途发展的新目标抗生素。的生物合成的关键是必要的吗原核生物的呼吸甲基萘醌类化合物,,途径仅限于一些细菌胃幽门螺杆菌病原体等物种幽门螺旋菌,这是一个潜在的目标具体抗生素。幽门螺旋杆菌methylthioadenosine的结构核苷酶(MTAN;特异性和活动对6-amino-6-deoxyfutalosine)参与甲基萘醌类生物合成的第二步阐明在分辨率为1.76 ?精制R因子R = 17%,免费的= 21%。活性位点突变体的水解6-amino-6-deoxyfutalosine遵循一种机制类似于大肠杆菌MTAN。提供的证据,这种模式的操作活性位点突变体的晶体结构。通过使用反应中间体结构给额外的证据先前提出的核苷酶机制。结构,证实了反应机理将提供一个基础结构设计的新的抑制剂针对futalosine通路。

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