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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis
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Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis

机译：结构的磷酸丝氨酸转氨酶结核分枝杆菌

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摘要

Mycobacterium tuberculosis (Mtb), the causative agent of TB, remains a serious world health problem owing to limitations of the available drugs and the emergence of resistant strains. In this context, key biosynthetic enzymes from Mtb are attractive targets for the development of new therapeutic drugs. Here, the 1.5 ? resolution crystal structure of Mtb phosphoserine aminotransferase (MtbPSAT) in complex with its cofactor, pyridoxal 5′-phosphate (PLP), is reported. MtbPSAT is an essential enzyme in the biosynthesis of serine and in pathways of one-carbon metabolism. The structure shows that although the Mtb enzyme differs substantially in sequence from other PSAT enzymes, its fold is conserved and its PLP-binding site is virtually identical. Structural comparisons suggest that this site remains unchanged throughout the catalytic cycle. On the other hand, PSAT enzymes are obligate dimers in which the two active sites are located in the dimer interface and distinct differences in the MtbPSAT dimer are noted. These impact on the substrate-binding region and access channel and suggest options for the development of selective inhibitors.
机译：结核分枝杆菌(Mtb)致病代理的结核病,世界仍然是一个严重的健康由于可用的局限性问题药物和耐药菌株的出现。这种情况下,结核分枝杆菌的生物合成的关键酶有吸引力的目标是开发新的吗治疗药物。结核分枝杆菌晶体结构的磷酸丝氨酸转氨酶(MtbPSAT)在复杂的代数余子式,吡哆醛5 '磷酸(PLP)报道。生物合成途径的丝氨酸和一个碳代谢。虽然Mtb酶显著不同从其他PSAT酶序列,其折叠守恒及其PLP-binding网站实际上是相同的。这个网站中保持不变催化循环。专二聚体中两个活跃的网站吗位于二聚体接口和不同MtbPSAT二聚体的差异。影响substrate-binding地区和访问发展通道和显示选项的选择性抑制剂。

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