Alice Dawson, Paul Trumper, Georgios Chrysostomou, William N Hunter
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引用次数: 0
摘要
双功能二氨基羟基磷核糖基氨基嘧啶脱氨酶/5-氨基-6-（5-磷核糖基氨基）尿嘧啶还原酶（RibD）是一种潜在的抗菌药物靶标。报告了重组鲍曼不动杆菌 RibD 的正方和四方晶体结构，分辨率分别为 2.2 Å 和 2.0 Å。与蛋白质数据库（Protein Data Bank）中的同源结构进行比较后发现两者非常相似。四方晶体是在存在单磷酸鸟苷的情况下获得的，令人惊讶的是观察到鸟苷占据了还原酶结构域的腺嘌呤结合位点。
Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii.
The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2 and 2.0 Å resolution, respectively. Comparisons with orthologous structures in the Protein Data Bank indicated close similarities. The tetragonal crystal form was obtained in the presence of guanosine monophosphate, which surprisingly was observed to occupy the adenine-binding site of the reductase domain.
期刊介绍：
Acta Crystallographica Section F is a rapid structural biology communications journal.
Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal.
The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles.
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